{"title":"Enzymes \u0026 Biochemicals","description":"","products":[{"product_id":"millipore-starch-go-p-assay-kit","title":"Starch (GO\/P) Assay Kit","description":"\u003cp\u003eStarch (GO\/P) Assay Kit — Sufficient for 20 Assays\u003c\/p\u003e\n\n\u003cp\u003eThe Starch (GO\/P) Assay Kit provides a reliable, enzymatic method for quantifying starch in food, feed, fermentation products, plant materials, and other complex matrices. Designed for routine lab workflows, this kit uses α-amylase, amyloglucosidase, glucose oxidase, peroxidase, and o-dianisidine to convert starch to glucose and generate a stable pink color measured at 540 nm.\u003c\/p\u003e\n\n\u003cp\u003eIdeal for quality control, R\u0026amp;D, agricultural analysis, brewing co-products, biomass evaluation, and academic research, this kit supports accurate starch determination without specialized instrumentation beyond a standard spectrophotometer.\u003c\/p\u003e\n\n\u003cp\u003eThis workflow mirrors the widely used GOPOD-based starch assay method and provides a practical alternative to higher-cost commercial starch assay kits.\u003c\/p\u003e","brand":"Millipore Sigma","offers":[{"title":"Default Title","offer_id":43042842214459,"sku":"STA20-1KT","price":445.0,"currency_code":"USD","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0606\/5641\/8875\/files\/STA20_8eebf867-7855-45e6-a97d-427d206ba513.png?v=1764188000"},{"product_id":"millipore-glucose-oxidase-aspergillus-niger-type7-10ku","title":"Glucose Oxidase from Aspergillus niger TypeVII - 10,000 units","description":"\u003cp\u003eGlucose Oxidase from Aspergillus niger\u003cbr\u003eType VII, lyophilized powder, ≥100,000 units\/g solid (without added oxygen)\u003cbr\u003eSynonym(s): β-D-Glucose:oxygen 1-oxidoreductase, G.Od., GOx\u003c\/p\u003e\n\u003cp\u003eGlucose Oxidase (Type VII) from Aspergillus niger is a high-activity, lyophilized enzyme preparation widely used across food analysis, diagnostics, biosensor development, bioprocessing, and academic research. This preparation delivers ≥100,000 units\/g solid (without added oxygen), providing strong performance for glucose quantification and coupled enzymatic assays.\u003cbr\u003e\u003c\/p\u003e\n\u003cp\u003eThe enzyme is a homodimer (~160 kDa) containing FAD as the essential cofactor for oxidation of β-D-glucose to D-glucono-β-lactone and hydrogen peroxide. With a pH optimum near 5.5 and a broad working range (pH 4–7), this preparation supports robust performance in a wide variety of analytical and manufacturing workflows.\u003cbr\u003eCommon applications include enzymatic glucose determination, biosensor fabrication, microfluidic devices, diagnostic assay manufacturing, and fuel-cell research. This material ships on wet ice and requires −20 °C storage.\u003c\/p\u003e","brand":"Millipore Sigma","offers":[{"title":"Default Title","offer_id":43042842345531,"sku":"G2133-10KU","price":89.13,"currency_code":"USD","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0606\/5641\/8875\/files\/G2133-10KU_c9dfca22-5655-4103-87b3-aed32e4f42c8.png?v=1764188001"},{"product_id":"millipore-glucose-oxidase-aspergillus-niger-type7-50ku","title":"Glucose Oxidase from Aspergillus niger TypeVII - 50,000 units","description":"\u003cp\u003eGlucose Oxidase from Aspergillus niger\u003cbr\u003eType VII, lyophilized powder, ≥100,000 units\/g solid (without added oxygen)\u003cbr\u003eSynonym(s): β-D-Glucose:oxygen 1-oxidoreductase, G.Od., GOx\u003c\/p\u003e\n\u003cp\u003eGlucose Oxidase (Type VII) from Aspergillus niger is a high-activity, lyophilized enzyme preparation widely used across food analysis, diagnostics, biosensor development, bioprocessing, and academic research. This preparation delivers ≥100,000 units\/g solid (without added oxygen), providing strong performance for glucose quantification and coupled enzymatic assays.\u003cbr\u003e\u003c\/p\u003e\n\u003cp\u003eThe enzyme is a homodimer (~160 kDa) containing FAD as the essential cofactor for oxidation of β-D-glucose to D-glucono-β-lactone and hydrogen peroxide. With a pH optimum near 5.5 and a broad working range (pH 4–7), this preparation supports robust performance in a wide variety of analytical and manufacturing workflows.\u003cbr\u003eCommon applications include enzymatic glucose determination, biosensor fabrication, microfluidic devices, diagnostic assay manufacturing, and fuel-cell research. This material ships on wet ice and requires −20 °C storage.\u003c\/p\u003e","brand":"Millipore Sigma","offers":[{"title":"Default Title","offer_id":43042842443835,"sku":"G2133-50KU","price":251.25,"currency_code":"USD","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0606\/5641\/8875\/files\/G2133-10KU_87fc40fa-ad3e-40fc-916b-1fd9190796aa.png?v=1764188001"},{"product_id":"millipore-glucose-oxidase-aspergillus-niger-type7-250ku","title":"Glucose Oxidase from Aspergillus niger TypeVII - 250,000 units","description":"\u003cp\u003eGlucose Oxidase from Aspergillus niger\u003cbr\u003eType VII, lyophilized powder, ≥100,000 units\/g solid (without added oxygen)\u003cbr\u003eSynonym(s): β-D-Glucose:oxygen 1-oxidoreductase, G.Od., GOx\u003c\/p\u003e\n\u003cp\u003eGlucose Oxidase (Type VII) from Aspergillus niger is a high-activity, lyophilized enzyme preparation widely used across food analysis, diagnostics, biosensor development, bioprocessing, and academic research. This preparation delivers ≥100,000 units\/g solid (without added oxygen), providing strong performance for glucose quantification and coupled enzymatic assays.\u003cbr\u003e\u003c\/p\u003e\n\u003cp\u003eThe enzyme is a homodimer (~160 kDa) containing FAD as the essential cofactor for oxidation of β-D-glucose to D-glucono-β-lactone and hydrogen peroxide. With a pH optimum near 5.5 and a broad working range (pH 4–7), this preparation supports robust performance in a wide variety of analytical and manufacturing workflows.\u003cbr\u003eCommon applications include enzymatic glucose determination, biosensor fabrication, microfluidic devices, diagnostic assay manufacturing, and fuel-cell research. This material ships on wet ice and requires −20 °C storage.\u003c\/p\u003e","brand":"Millipore Sigma","offers":[{"title":"Default Title","offer_id":43042842542139,"sku":"G2133-250KU","price":811.25,"currency_code":"USD","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0606\/5641\/8875\/files\/G2133-10KU_4018f34c-4c3e-4918-b797-628189247fcb.png?v=1764188002"},{"product_id":"millipore-glucose-oxidase-aspergillus-niger-type7-25mu","title":"Glucose Oxidase from Aspergillus niger TypeVII -  2,500,000 units","description":"\u003cp\u003eGlucose Oxidase from Aspergillus niger\u003cbr\u003eType VII, lyophilized powder, ≥100,000 units\/g solid (without added oxygen)\u003cbr\u003eSynonym(s): β-D-Glucose:oxygen 1-oxidoreductase, G.Od., GOx\u003c\/p\u003e\n\u003cp\u003eGlucose Oxidase (Type VII) from Aspergillus niger is a high-activity, lyophilized enzyme preparation widely used across food analysis, diagnostics, biosensor development, bioprocessing, and academic research. This preparation delivers ≥100,000 units\/g solid (without added oxygen), providing strong performance for glucose quantification and coupled enzymatic assays.\u003cbr\u003e\u003c\/p\u003e\n\u003cp\u003eThe enzyme is a homodimer (~160 kDa) containing FAD as the essential cofactor for oxidation of β-D-glucose to D-glucono-β-lactone and hydrogen peroxide. With a pH optimum near 5.5 and a broad working range (pH 4–7), this preparation supports robust performance in a wide variety of analytical and manufacturing workflows.\u003cbr\u003eCommon applications include enzymatic glucose determination, biosensor fabrication, microfluidic devices, diagnostic assay manufacturing, and fuel-cell research. This material ships on wet ice and requires −20 °C storage.\u003c\/p\u003e","brand":"Millipore Sigma","offers":[{"title":"Default Title","offer_id":43042842673211,"sku":"G2133-2.5MU","price":5700.0,"currency_code":"USD","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0606\/5641\/8875\/files\/G2133-10KU_ae3a88e4-7b40-4fbc-b1f9-9ad98fe9880e.png?v=1764188003"},{"product_id":"millipore-peroxidase-horseradish-type6-1000u","title":"Peroxidase from horseradish Type VI - 1000 units","description":"\u003cp\u003ePeroxidase from horseradish\u003cbr\u003e\nType VI, essentially salt-free, lyophilized powder, ≥250 units\/mg solid (using pyrogallol)\u003c\/p\u003e\n\n\u003cp\u003eSynonym(s):\u003cbr\u003e\nDetection Enzyme, HRP, Peroxidase, Donor:hydrogen-peroxide oxidoreductase, Horseradish peroxidase\u003c\/p\u003e\n\n\u003cp\u003eGeneral description\u003cbr\u003e\nHorseradish peroxidase is isolated from horseradish roots (Amoracia rusticana) and belongs to the ferroprotoporphyrin group of peroxidases. HRP is a single chain polypeptide containing four disulfide bridges. It is a glycoprotein containing 18% carbohydrate. The carbohydrate composition consists of galactose, arabinose, xylose, fucose, mannose, mannosamine, and galactosamine depending upon the specific isozyme. Its molecular weight (~44 kDa) includes the polypeptide chain (33,890 Daltons), hemin plus Ca2+ (~700 Daltons), and carbohydrate (~9,400 Daltons). At least seven isozymes of HRP exist. The isoelectric point for horseradish peroxidase isozymes ranges from 3.0 - 9.0.\u003c\/p\u003e\n\n\u003cp\u003eApplication\u003cbr\u003e\nHorseradish peroxidase (HRP) is isolated from horseradish roots (Amoracia rusticana) and belongs to the ferroprotoporphyrin group of peroxidases.. It is used in biochemistry applications such as western blots, ELISA and Immunohistochemistry. Horseradish peroxidase is used to amplify a weak signal and increase detectability of a target molecule, such as a protein. Product P8375, type VI, is an essentially salt free lyophilized powder. It is commonly used to determine amounts of glucose and peroxides in solution. It has been used to study sensory input of cervical spinal cord neurons[1].\u003c\/p\u003e\n\n\u003cp\u003eThe enzyme has been used to develop a thermostable soybean peroxidase-based biosensor by cross-linking and electrically ′wiring′ the enzyme through a redox-conducting hydrogel to a glassy carbon electrode.[2] It has also been used to assay the oxidation of low density lipoprotein.[3]\u003c\/p\u003e\n\n\u003cp\u003eBiochem\/physiol Actions\u003cbr\u003e\nHRP readily combines with hydrogen peroxide (H2O2) and the resultant [HRP-H2O2] complex can oxidize a wide variety of hydrogen donors. The optimal pH is 6.0-6.5 and the enzyme is most stable in the pH range of 5.0-9.0. HRP can be conjugated to antibodies by several different methods including glutaraldehyde, periodate oxidation, through disulfide bonds, and also via amino and thiol directed cross-linkers. It is smaller and more stable than the enzyme labels β-galactosidase and alkaline phosphatase and hence, it is the most desired label. Also, its glycosylation leads to lower non-specific binding.[4]\u003cbr\u003e\nWhen incubated with a substrate, horseradish peroxidase produces a coloured, fluorimetric, or luminescent derivative of the labeled molecule, allowing quantification. Horseradish peroxidase has been shown to slightly reduce the level of inhibition in a cydAB mutant. Known inhibitors are sodium azide, cyanide, L-cystine, dichromate, ethylenethiourea, hydroxylamine, sulfide, vanadate, p-aminobenzoic acid, and Cd2+, Co2+, Cu2+, Fe3+, Mn2+, Ni2+, and Pb2+ ions.\u003c\/p\u003e\n\n\u003cp\u003eAnalysis Note\u003cbr\u003e\nThe RZ (Reinheitszahl) is the absorbance ratio A403\/A275 determined at 0.5-1.0 mg\/ml in deionized water. It is a measure of hemin content, not enzymatic activity. Even preparations with high RZ may have low enzymatic activity.\u003c\/p\u003e\n\n\u003cp\u003eOther Notes\u003cbr\u003e\nOne pyrogallol unit will form 1.0 mg purpurogallin from pyrogallol in 20 sec at pH 6.0 at 20 °C.\u003c\/p\u003e","brand":"Millipore Sigma","offers":[{"title":"Default Title","offer_id":43042843459643,"sku":"P8375-1KU","price":82.0,"currency_code":"USD","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0606\/5641\/8875\/files\/P8375-10KU_05782490-e3ee-4334-871e-0f5c5b1a7390.png?v=1764188012"},{"product_id":"millipore-peroxidase-horseradish-type6-2000u","title":"Peroxidase from horseradish Type VI - 2000 units","description":"\u003cp\u003ePeroxidase from horseradish\u003cbr\u003e\nType VI, essentially salt-free, lyophilized powder, ≥250 units\/mg solid (using pyrogallol)\u003c\/p\u003e\n\n\u003cp\u003eSynonym(s):\u003cbr\u003e\nDetection Enzyme, HRP, Peroxidase, Donor:hydrogen-peroxide oxidoreductase, Horseradish peroxidase\u003c\/p\u003e\n\n\u003cp\u003eGeneral description\u003cbr\u003e\nHorseradish peroxidase is isolated from horseradish roots (Amoracia rusticana) and belongs to the ferroprotoporphyrin group of peroxidases. HRP is a single chain polypeptide containing four disulfide bridges. It is a glycoprotein containing 18% carbohydrate. The carbohydrate composition consists of galactose, arabinose, xylose, fucose, mannose, mannosamine, and galactosamine depending upon the specific isozyme. Its molecular weight (~44 kDa) includes the polypeptide chain (33,890 Daltons), hemin plus Ca2+ (~700 Daltons), and carbohydrate (~9,400 Daltons). At least seven isozymes of HRP exist. The isoelectric point for horseradish peroxidase isozymes ranges from 3.0 - 9.0.\u003c\/p\u003e\n\n\u003cp\u003eApplication\u003cbr\u003e\nHorseradish peroxidase (HRP) is isolated from horseradish roots (Amoracia rusticana) and belongs to the ferroprotoporphyrin group of peroxidases.. It is used in biochemistry applications such as western blots, ELISA and Immunohistochemistry. Horseradish peroxidase is used to amplify a weak signal and increase detectability of a target molecule, such as a protein. Product P8375, type VI, is an essentially salt free lyophilized powder. It is commonly used to determine amounts of glucose and peroxides in solution. It has been used to study sensory input of cervical spinal cord neurons[1].\u003c\/p\u003e\n\n\u003cp\u003eThe enzyme has been used to develop a thermostable soybean peroxidase-based biosensor by cross-linking and electrically ′wiring′ the enzyme through a redox-conducting hydrogel to a glassy carbon electrode.[2] It has also been used to assay the oxidation of low density lipoprotein.[3]\u003c\/p\u003e\n\n\u003cp\u003eBiochem\/physiol Actions\u003cbr\u003e\nHRP readily combines with hydrogen peroxide (H2O2) and the resultant [HRP-H2O2] complex can oxidize a wide variety of hydrogen donors. The optimal pH is 6.0-6.5 and the enzyme is most stable in the pH range of 5.0-9.0. HRP can be conjugated to antibodies by several different methods including glutaraldehyde, periodate oxidation, through disulfide bonds, and also via amino and thiol directed cross-linkers. It is smaller and more stable than the enzyme labels β-galactosidase and alkaline phosphatase and hence, it is the most desired label. Also, its glycosylation leads to lower non-specific binding.[4]\u003cbr\u003e\nWhen incubated with a substrate, horseradish peroxidase produces a coloured, fluorimetric, or luminescent derivative of the labeled molecule, allowing quantification. Horseradish peroxidase has been shown to slightly reduce the level of inhibition in a cydAB mutant. Known inhibitors are sodium azide, cyanide, L-cystine, dichromate, ethylenethiourea, hydroxylamine, sulfide, vanadate, p-aminobenzoic acid, and Cd2+, Co2+, Cu2+, Fe3+, Mn2+, Ni2+, and Pb2+ ions.\u003c\/p\u003e\n\n\u003cp\u003eAnalysis Note\u003cbr\u003e\nThe RZ (Reinheitszahl) is the absorbance ratio A403\/A275 determined at 0.5-1.0 mg\/ml in deionized water. It is a measure of hemin content, not enzymatic activity. Even preparations with high RZ may have low enzymatic activity.\u003c\/p\u003e\n\n\u003cp\u003eOther Notes\u003cbr\u003e\nOne pyrogallol unit will form 1.0 mg purpurogallin from pyrogallol in 20 sec at pH 6.0 at 20 °C.\u003c\/p\u003e","brand":"Millipore Sigma","offers":[{"title":"Default Title","offer_id":43042843557947,"sku":"P8375-2KU","price":132.5,"currency_code":"USD","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0606\/5641\/8875\/files\/P8375-10KU_57b936e5-6c34-44e1-8c89-d7642d0b3c6f.png?v=1764188012"},{"product_id":"millipore-peroxidase-horseradish-type6-5000u","title":"Peroxidase from horseradish Type VI -5000 units","description":"\u003cp\u003ePeroxidase from horseradish\u003cbr\u003e\nType VI, essentially salt-free, lyophilized powder, ≥250 units\/mg solid (using pyrogallol)\u003c\/p\u003e\n\n\u003cp\u003eSynonym(s):\u003cbr\u003e\nDetection Enzyme, HRP, Peroxidase, Donor:hydrogen-peroxide oxidoreductase, Horseradish peroxidase\u003c\/p\u003e\n\n\u003cp\u003eGeneral description\u003cbr\u003e\nHorseradish peroxidase is isolated from horseradish roots (Amoracia rusticana) and belongs to the ferroprotoporphyrin group of peroxidases. HRP is a single chain polypeptide containing four disulfide bridges. It is a glycoprotein containing 18% carbohydrate. The carbohydrate composition consists of galactose, arabinose, xylose, fucose, mannose, mannosamine, and galactosamine depending upon the specific isozyme. Its molecular weight (~44 kDa) includes the polypeptide chain (33,890 Daltons), hemin plus Ca2+ (~700 Daltons), and carbohydrate (~9,400 Daltons). At least seven isozymes of HRP exist. The isoelectric point for horseradish peroxidase isozymes ranges from 3.0 - 9.0.\u003c\/p\u003e\n\n\u003cp\u003eApplication\u003cbr\u003e\nHorseradish peroxidase (HRP) is isolated from horseradish roots (Amoracia rusticana) and belongs to the ferroprotoporphyrin group of peroxidases.. It is used in biochemistry applications such as western blots, ELISA and Immunohistochemistry. Horseradish peroxidase is used to amplify a weak signal and increase detectability of a target molecule, such as a protein. Product P8375, type VI, is an essentially salt free lyophilized powder. It is commonly used to determine amounts of glucose and peroxides in solution. It has been used to study sensory input of cervical spinal cord neurons[1].\u003c\/p\u003e\n\n\u003cp\u003eThe enzyme has been used to develop a thermostable soybean peroxidase-based biosensor by cross-linking and electrically ′wiring′ the enzyme through a redox-conducting hydrogel to a glassy carbon electrode.[2] It has also been used to assay the oxidation of low density lipoprotein.[3]\u003c\/p\u003e\n\n\u003cp\u003eBiochem\/physiol Actions\u003cbr\u003e\nHRP readily combines with hydrogen peroxide (H2O2) and the resultant [HRP-H2O2] complex can oxidize a wide variety of hydrogen donors. The optimal pH is 6.0-6.5 and the enzyme is most stable in the pH range of 5.0-9.0. HRP can be conjugated to antibodies by several different methods including glutaraldehyde, periodate oxidation, through disulfide bonds, and also via amino and thiol directed cross-linkers. It is smaller and more stable than the enzyme labels β-galactosidase and alkaline phosphatase and hence, it is the most desired label. Also, its glycosylation leads to lower non-specific binding.[4]\u003cbr\u003e\nWhen incubated with a substrate, horseradish peroxidase produces a coloured, fluorimetric, or luminescent derivative of the labeled molecule, allowing quantification. Horseradish peroxidase has been shown to slightly reduce the level of inhibition in a cydAB mutant. Known inhibitors are sodium azide, cyanide, L-cystine, dichromate, ethylenethiourea, hydroxylamine, sulfide, vanadate, p-aminobenzoic acid, and Cd2+, Co2+, Cu2+, Fe3+, Mn2+, Ni2+, and Pb2+ ions.\u003c\/p\u003e\n\n\u003cp\u003eAnalysis Note\u003cbr\u003e\nThe RZ (Reinheitszahl) is the absorbance ratio A403\/A275 determined at 0.5-1.0 mg\/ml in deionized water. It is a measure of hemin content, not enzymatic activity. Even preparations with high RZ may have low enzymatic activity.\u003c\/p\u003e\n\n\u003cp\u003eOther Notes\u003cbr\u003e\nOne pyrogallol unit will form 1.0 mg purpurogallin from pyrogallol in 20 sec at pH 6.0 at 20 °C.\u003c\/p\u003e","brand":"Millipore Sigma","offers":[{"title":"Default Title","offer_id":43042843623483,"sku":"P8375-5KU","price":152.5,"currency_code":"USD","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0606\/5641\/8875\/files\/P8375-10KU_211f5a46-19a1-4d33-bc84-8f120e7a882d.png?v=1764188013"},{"product_id":"millipore-peroxidase-horseradish-type6-10ku","title":"Peroxidase from horseradish Type VI - 10,000 units","description":"\u003cp\u003ePeroxidase from horseradish\u003cbr\u003e\nType VI, essentially salt-free, lyophilized powder, ≥250 units\/mg solid (using pyrogallol)\u003c\/p\u003e\n\n\u003cp\u003eSynonym(s):\u003cbr\u003e\nDetection Enzyme, HRP, Peroxidase, Donor:hydrogen-peroxide oxidoreductase, Horseradish peroxidase\u003c\/p\u003e\n\n\u003cp\u003eGeneral description\u003cbr\u003e\nHorseradish peroxidase is isolated from horseradish roots (Amoracia rusticana) and belongs to the ferroprotoporphyrin group of peroxidases. HRP is a single chain polypeptide containing four disulfide bridges. It is a glycoprotein containing 18% carbohydrate. The carbohydrate composition consists of galactose, arabinose, xylose, fucose, mannose, mannosamine, and galactosamine depending upon the specific isozyme. Its molecular weight (~44 kDa) includes the polypeptide chain (33,890 Daltons), hemin plus Ca2+ (~700 Daltons), and carbohydrate (~9,400 Daltons). At least seven isozymes of HRP exist. The isoelectric point for horseradish peroxidase isozymes ranges from 3.0 - 9.0.\u003c\/p\u003e\n\n\u003cp\u003eApplication\u003cbr\u003e\nHorseradish peroxidase (HRP) is isolated from horseradish roots (Amoracia rusticana) and belongs to the ferroprotoporphyrin group of peroxidases.. It is used in biochemistry applications such as western blots, ELISA and Immunohistochemistry. Horseradish peroxidase is used to amplify a weak signal and increase detectability of a target molecule, such as a protein. Product P8375, type VI, is an essentially salt free lyophilized powder. It is commonly used to determine amounts of glucose and peroxides in solution. It has been used to study sensory input of cervical spinal cord neurons[1].\u003c\/p\u003e\n\n\u003cp\u003eThe enzyme has been used to develop a thermostable soybean peroxidase-based biosensor by cross-linking and electrically ′wiring′ the enzyme through a redox-conducting hydrogel to a glassy carbon electrode.[2] It has also been used to assay the oxidation of low density lipoprotein.[3]\u003c\/p\u003e\n\n\u003cp\u003eBiochem\/physiol Actions\u003cbr\u003e\nHRP readily combines with hydrogen peroxide (H2O2) and the resultant [HRP-H2O2] complex can oxidize a wide variety of hydrogen donors. The optimal pH is 6.0-6.5 and the enzyme is most stable in the pH range of 5.0-9.0. HRP can be conjugated to antibodies by several different methods including glutaraldehyde, periodate oxidation, through disulfide bonds, and also via amino and thiol directed cross-linkers. It is smaller and more stable than the enzyme labels β-galactosidase and alkaline phosphatase and hence, it is the most desired label. Also, its glycosylation leads to lower non-specific binding.[4]\u003cbr\u003e\nWhen incubated with a substrate, horseradish peroxidase produces a coloured, fluorimetric, or luminescent derivative of the labeled molecule, allowing quantification. Horseradish peroxidase has been shown to slightly reduce the level of inhibition in a cydAB mutant. Known inhibitors are sodium azide, cyanide, L-cystine, dichromate, ethylenethiourea, hydroxylamine, sulfide, vanadate, p-aminobenzoic acid, and Cd2+, Co2+, Cu2+, Fe3+, Mn2+, Ni2+, and Pb2+ ions.\u003c\/p\u003e\n\n\u003cp\u003eAnalysis Note\u003cbr\u003e\nThe RZ (Reinheitszahl) is the absorbance ratio A403\/A275 determined at 0.5-1.0 mg\/ml in deionized water. It is a measure of hemin content, not enzymatic activity. Even preparations with high RZ may have low enzymatic activity.\u003c\/p\u003e\n\n\u003cp\u003eOther Notes\u003cbr\u003e\nOne pyrogallol unit will form 1.0 mg purpurogallin from pyrogallol in 20 sec at pH 6.0 at 20 °C.\u003c\/p\u003e","brand":"Millipore Sigma","offers":[{"title":"Default Title","offer_id":43042843721787,"sku":"P8375-10KU","price":327.5,"currency_code":"USD","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0606\/5641\/8875\/files\/P8375-10KU_22b233bd-6f72-4982-9b4b-0b2e391f3a27.png?v=1764188014"},{"product_id":"millipore-peroxidase-horseradish-type6-25ku","title":"Peroxidase from horseradish Type VI - 25,000 units","description":"\u003cp\u003ePeroxidase from horseradish\u003cbr\u003e\nType VI, essentially salt-free, lyophilized powder, ≥250 units\/mg solid (using pyrogallol)\u003c\/p\u003e\n\n\u003cp\u003eSynonym(s):\u003cbr\u003e\nDetection Enzyme, HRP, Peroxidase, Donor:hydrogen-peroxide oxidoreductase, Horseradish peroxidase\u003c\/p\u003e\n\n\u003cp\u003eGeneral description\u003cbr\u003e\nHorseradish peroxidase is isolated from horseradish roots (Amoracia rusticana) and belongs to the ferroprotoporphyrin group of peroxidases. HRP is a single chain polypeptide containing four disulfide bridges. It is a glycoprotein containing 18% carbohydrate. The carbohydrate composition consists of galactose, arabinose, xylose, fucose, mannose, mannosamine, and galactosamine depending upon the specific isozyme. Its molecular weight (~44 kDa) includes the polypeptide chain (33,890 Daltons), hemin plus Ca2+ (~700 Daltons), and carbohydrate (~9,400 Daltons). At least seven isozymes of HRP exist. The isoelectric point for horseradish peroxidase isozymes ranges from 3.0 - 9.0.\u003c\/p\u003e\n\n\u003cp\u003eApplication\u003cbr\u003e\nHorseradish peroxidase (HRP) is isolated from horseradish roots (Amoracia rusticana) and belongs to the ferroprotoporphyrin group of peroxidases.. It is used in biochemistry applications such as western blots, ELISA and Immunohistochemistry. Horseradish peroxidase is used to amplify a weak signal and increase detectability of a target molecule, such as a protein. Product P8375, type VI, is an essentially salt free lyophilized powder. It is commonly used to determine amounts of glucose and peroxides in solution. It has been used to study sensory input of cervical spinal cord neurons[1].\u003c\/p\u003e\n\n\u003cp\u003eThe enzyme has been used to develop a thermostable soybean peroxidase-based biosensor by cross-linking and electrically ′wiring′ the enzyme through a redox-conducting hydrogel to a glassy carbon electrode.[2] It has also been used to assay the oxidation of low density lipoprotein.[3]\u003c\/p\u003e\n\n\u003cp\u003eBiochem\/physiol Actions\u003cbr\u003e\nHRP readily combines with hydrogen peroxide (H2O2) and the resultant [HRP-H2O2] complex can oxidize a wide variety of hydrogen donors. The optimal pH is 6.0-6.5 and the enzyme is most stable in the pH range of 5.0-9.0. HRP can be conjugated to antibodies by several different methods including glutaraldehyde, periodate oxidation, through disulfide bonds, and also via amino and thiol directed cross-linkers. It is smaller and more stable than the enzyme labels β-galactosidase and alkaline phosphatase and hence, it is the most desired label. Also, its glycosylation leads to lower non-specific binding.[4]\u003cbr\u003e\nWhen incubated with a substrate, horseradish peroxidase produces a coloured, fluorimetric, or luminescent derivative of the labeled molecule, allowing quantification. Horseradish peroxidase has been shown to slightly reduce the level of inhibition in a cydAB mutant. Known inhibitors are sodium azide, cyanide, L-cystine, dichromate, ethylenethiourea, hydroxylamine, sulfide, vanadate, p-aminobenzoic acid, and Cd2+, Co2+, Cu2+, Fe3+, Mn2+, Ni2+, and Pb2+ ions.\u003c\/p\u003e\n\n\u003cp\u003eAnalysis Note\u003cbr\u003e\nThe RZ (Reinheitszahl) is the absorbance ratio A403\/A275 determined at 0.5-1.0 mg\/ml in deionized water. It is a measure of hemin content, not enzymatic activity. Even preparations with high RZ may have low enzymatic activity.\u003c\/p\u003e\n\n\u003cp\u003eOther Notes\u003cbr\u003e\nOne pyrogallol unit will form 1.0 mg purpurogallin from pyrogallol in 20 sec at pH 6.0 at 20 °C.\u003c\/p\u003e","brand":"Millipore Sigma","offers":[{"title":"Default Title","offer_id":43042843787323,"sku":"P8375-25KU","price":560.0,"currency_code":"USD","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0606\/5641\/8875\/files\/P8375-25KU_f04e475a-0717-446f-8226-330032219b76.png?v=1764188015"},{"product_id":"millipore-peroxidase-horseradish-type6-100ku","title":"Peroxidase from horseradish Type VI - 100,000 units","description":"\u003cp\u003ePeroxidase from horseradish\u003cbr\u003e\nType VI, essentially salt-free, lyophilized powder, ≥250 units\/mg solid (using pyrogallol)\u003c\/p\u003e\n\n\u003cp\u003eSynonym(s):\u003cbr\u003e\nDetection Enzyme, HRP, Peroxidase, Donor:hydrogen-peroxide oxidoreductase, Horseradish peroxidase\u003c\/p\u003e\n\n\u003cp\u003eGeneral description\u003cbr\u003e\nHorseradish peroxidase is isolated from horseradish roots (Amoracia rusticana) and belongs to the ferroprotoporphyrin group of peroxidases. HRP is a single chain polypeptide containing four disulfide bridges. It is a glycoprotein containing 18% carbohydrate. The carbohydrate composition consists of galactose, arabinose, xylose, fucose, mannose, mannosamine, and galactosamine depending upon the specific isozyme. Its molecular weight (~44 kDa) includes the polypeptide chain (33,890 Daltons), hemin plus Ca2+ (~700 Daltons), and carbohydrate (~9,400 Daltons). At least seven isozymes of HRP exist. The isoelectric point for horseradish peroxidase isozymes ranges from 3.0 - 9.0.\u003c\/p\u003e\n\n\u003cp\u003eApplication\u003cbr\u003e\nHorseradish peroxidase (HRP) is isolated from horseradish roots (Amoracia rusticana) and belongs to the ferroprotoporphyrin group of peroxidases.. It is used in biochemistry applications such as western blots, ELISA and Immunohistochemistry. Horseradish peroxidase is used to amplify a weak signal and increase detectability of a target molecule, such as a protein. Product P8375, type VI, is an essentially salt free lyophilized powder. It is commonly used to determine amounts of glucose and peroxides in solution. It has been used to study sensory input of cervical spinal cord neurons[1].\u003c\/p\u003e\n\n\u003cp\u003eThe enzyme has been used to develop a thermostable soybean peroxidase-based biosensor by cross-linking and electrically ′wiring′ the enzyme through a redox-conducting hydrogel to a glassy carbon electrode.[2] It has also been used to assay the oxidation of low density lipoprotein.[3]\u003c\/p\u003e\n\n\u003cp\u003eBiochem\/physiol Actions\u003cbr\u003e\nHRP readily combines with hydrogen peroxide (H2O2) and the resultant [HRP-H2O2] complex can oxidize a wide variety of hydrogen donors. The optimal pH is 6.0-6.5 and the enzyme is most stable in the pH range of 5.0-9.0. HRP can be conjugated to antibodies by several different methods including glutaraldehyde, periodate oxidation, through disulfide bonds, and also via amino and thiol directed cross-linkers. It is smaller and more stable than the enzyme labels β-galactosidase and alkaline phosphatase and hence, it is the most desired label. Also, its glycosylation leads to lower non-specific binding.[4]\u003cbr\u003e\nWhen incubated with a substrate, horseradish peroxidase produces a coloured, fluorimetric, or luminescent derivative of the labeled molecule, allowing quantification. Horseradish peroxidase has been shown to slightly reduce the level of inhibition in a cydAB mutant. Known inhibitors are sodium azide, cyanide, L-cystine, dichromate, ethylenethiourea, hydroxylamine, sulfide, vanadate, p-aminobenzoic acid, and Cd2+, Co2+, Cu2+, Fe3+, Mn2+, Ni2+, and Pb2+ ions.\u003c\/p\u003e\n\n\u003cp\u003eAnalysis Note\u003cbr\u003e\nThe RZ (Reinheitszahl) is the absorbance ratio A403\/A275 determined at 0.5-1.0 mg\/ml in deionized water. It is a measure of hemin content, not enzymatic activity. Even preparations with high RZ may have low enzymatic activity.\u003c\/p\u003e\n\n\u003cp\u003eOther Notes\u003cbr\u003e\nOne pyrogallol unit will form 1.0 mg purpurogallin from pyrogallol in 20 sec at pH 6.0 at 20 °C.\u003c\/p\u003e","brand":"Millipore Sigma","offers":[{"title":"Default Title","offer_id":43042843885627,"sku":"P8375-100KU","price":2375.0,"currency_code":"USD","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0606\/5641\/8875\/files\/P8375-100KU_3c207842-172d-4e75-9eff-3ac38c80c2b1.png?v=1764188015"},{"product_id":"millipore-peroxidase-horseradish-type6-250ku","title":"Peroxidase from horseradish Type VI - 250,000 units","description":"\u003cp\u003ePeroxidase from horseradish\u003cbr\u003e\nType VI, essentially salt-free, lyophilized powder, ≥250 units\/mg solid (using pyrogallol)\u003c\/p\u003e\n\n\u003cp\u003eSynonym(s):\u003cbr\u003e\nDetection Enzyme, HRP, Peroxidase, Donor:hydrogen-peroxide oxidoreductase, Horseradish peroxidase\u003c\/p\u003e\n\n\u003cp\u003eGeneral description\u003cbr\u003e\nHorseradish peroxidase is isolated from horseradish roots (Amoracia rusticana) and belongs to the ferroprotoporphyrin group of peroxidases. HRP is a single chain polypeptide containing four disulfide bridges. It is a glycoprotein containing 18% carbohydrate. The carbohydrate composition consists of galactose, arabinose, xylose, fucose, mannose, mannosamine, and galactosamine depending upon the specific isozyme. Its molecular weight (~44 kDa) includes the polypeptide chain (33,890 Daltons), hemin plus Ca2+ (~700 Daltons), and carbohydrate (~9,400 Daltons). At least seven isozymes of HRP exist. The isoelectric point for horseradish peroxidase isozymes ranges from 3.0 - 9.0.\u003c\/p\u003e\n\n\u003cp\u003eApplication\u003cbr\u003e\nHorseradish peroxidase (HRP) is isolated from horseradish roots (Amoracia rusticana) and belongs to the ferroprotoporphyrin group of peroxidases.. It is used in biochemistry applications such as western blots, ELISA and Immunohistochemistry. Horseradish peroxidase is used to amplify a weak signal and increase detectability of a target molecule, such as a protein. Product P8375, type VI, is an essentially salt free lyophilized powder. It is commonly used to determine amounts of glucose and peroxides in solution. It has been used to study sensory input of cervical spinal cord neurons[1].\u003c\/p\u003e\n\n\u003cp\u003eThe enzyme has been used to develop a thermostable soybean peroxidase-based biosensor by cross-linking and electrically ′wiring′ the enzyme through a redox-conducting hydrogel to a glassy carbon electrode.[2] It has also been used to assay the oxidation of low density lipoprotein.[3]\u003c\/p\u003e\n\n\u003cp\u003eBiochem\/physiol Actions\u003cbr\u003e\nHRP readily combines with hydrogen peroxide (H2O2) and the resultant [HRP-H2O2] complex can oxidize a wide variety of hydrogen donors. The optimal pH is 6.0-6.5 and the enzyme is most stable in the pH range of 5.0-9.0. HRP can be conjugated to antibodies by several different methods including glutaraldehyde, periodate oxidation, through disulfide bonds, and also via amino and thiol directed cross-linkers. It is smaller and more stable than the enzyme labels β-galactosidase and alkaline phosphatase and hence, it is the most desired label. Also, its glycosylation leads to lower non-specific binding.[4]\u003cbr\u003e\nWhen incubated with a substrate, horseradish peroxidase produces a coloured, fluorimetric, or luminescent derivative of the labeled molecule, allowing quantification. Horseradish peroxidase has been shown to slightly reduce the level of inhibition in a cydAB mutant. Known inhibitors are sodium azide, cyanide, L-cystine, dichromate, ethylenethiourea, hydroxylamine, sulfide, vanadate, p-aminobenzoic acid, and Cd2+, Co2+, Cu2+, Fe3+, Mn2+, Ni2+, and Pb2+ ions.\u003c\/p\u003e\n\n\u003cp\u003eAnalysis Note\u003cbr\u003e\nThe RZ (Reinheitszahl) is the absorbance ratio A403\/A275 determined at 0.5-1.0 mg\/ml in deionized water. It is a measure of hemin content, not enzymatic activity. Even preparations with high RZ may have low enzymatic activity.\u003c\/p\u003e\n\n\u003cp\u003eOther Notes\u003cbr\u003e\nOne pyrogallol unit will form 1.0 mg purpurogallin from pyrogallol in 20 sec at pH 6.0 at 20 °C.\u003c\/p\u003e","brand":"Millipore Sigma","offers":[{"title":"Default Title","offer_id":43042843951163,"sku":"P8375-250KU","price":4537.5,"currency_code":"USD","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0606\/5641\/8875\/files\/P8375-100KU_4106b60e-4b21-4a95-b870-4dc2d72c96c2.png?v=1764188016"},{"product_id":"millipore-peroxidase-horseradish-type6a-5mg","title":"Peroxidase from horseradish Type VI-A - 5MG","description":"\u003cp\u003ePeroxidase from horseradish - 5MG\u003cbr\u003e\nType VI-A, essentially salt-free, lyophilized powder, 950-2000 units\/mg solid (using ABTS), ≥250 units\/mg solid (using pyrogallol)\u003c\/p\u003e\n\n\u003cp\u003eSynonym(s): Donor:hydrogen-peroxide oxidoreductase, Horseradish peroxidase\u003c\/p\u003e\n\n\u003cp\u003eGeneral description\u003cbr\u003e\nHorseradish peroxidase is isolated from horseradish roots (Amoracia rusticana) and belongs to the ferroprotoporphyrin group of peroxidases. HRP is a single chain polypeptide containing four disulfide bridges. It is a glycoprotein containing 18% carbohydrate. The carbohydrate composition consists of galactose, arabinose, xylose, fucose, mannose, mannosamine, and galactosamine depending upon the specific isozyme. Its molecular weight (~44 kDa) includes the polypeptide chain (33,890 Daltons), hemin plus Ca2+ (~700 Daltons), and carbohydrate (~9,400 Daltons). At least seven isozymes of HRP exist. The isoelectric point for horseradish peroxidase isozymes ranges from 3.0 - 9.0.\u003c\/p\u003e\n\n\u003cp\u003eApplication\u003cbr\u003e\nHorseradish peroxidase (HRP) is isolated from horseradish roots (Amoracia rusticana). It is used in biochemistry applications such as western blots, ELISA and Immunohistochemistry. Horseradish peroxidase is used to amplify a weak signal and increase detectability of a target molecule, such as a protein. Product P6782 is type VI-A and it is essentially a salt-free, lyophilized powder. It is used to quantify cholesterol and cholesterol esters[1] and to study in vitro lipid deposition on hydrogel and silicone hydrogel contact lenses[2].\u003c\/p\u003e\n\n\u003cp\u003eThe enzyme from Sigma has been used in the development of rapid and sensitive galactose oxidase-peroxidase biosensor for galactose detection with prolonged stability.[3] It has been used as a component of a media (MRS agar) plate containing 3,3′,5,5′-tetramethylbenzidine (TMB) for the growth of Lactobacillus sp. TMB acts as a chromogenic substrate of peroxidase. Peroxidase generates O2 from H2O2 produced by the lactobacilli, and the TMB stains the colonies blue in the presence of O2. Thus, after 48 hours of incubation under 5% CO2 in air, the colonies that produce H2O2 on MRS agar appear dark blue. H2O2 nonproducers are colorless.[4] It has been used to study the stabilization effect of polyvinyl alcohol on horseradish peroxidase.[5] It is also used for the determination of glucose[6] and peroxides[7] in solution.\u003c\/p\u003e\n\n\u003cp\u003eBiochem\/physiol Actions\u003cbr\u003e\nHRP readily combines with hydrogen peroxide (H2O2) and the resultant [HRP-H2O2] complex can oxidize a wide variety of hydrogen donors. The optimal pH is 6.0-6.5 and the enzyme is most stable in the pH range of 5.0-9.0. HRP can be conjugated to antibodies by several different methods that include the use of glutaraldehyde, periodate oxidation, disulfide bonds, and also via amino and thiol directed cross-linkers. It is smaller and more stable than the enzyme labels, β-galactosidase and alkaline phosphatase. Hence, it is the most desired label. Also, its glycosylation leads to lower non-specific binding.[8] Sodium azide, cyanide, L-cystine, dichromate, ethylenethiourea, hydroxylamine, sulfide, vanadate, p-aminobenzoic acid, as well as Cd2+, Co2+, Cu2+, Fe3+, Mn2+, Ni2+, and Pb2+ ions are found to inhibit the enzyme activity.[9]\u003c\/p\u003e\n\n\u003cp\u003eWhen incubated with a substrate, horseradish peroxidase produces a coloured, fluorimetric, or luminescent derivative of the labeled molecule, allowing quantification. Horseradish peroxidase has been shown to slightly reduce the level of inhibition in a cydAB mutant.\u003c\/p\u003e\n\n\u003cp\u003ePackaging\u003cbr\u003e\nPackaged in mg solid\u003c\/p\u003e\n\n\u003cp\u003ePreparation Note\u003cbr\u003e\nSolutions of this product at 1 mg\/mL in 0.1 M phosphate buffer (pH 6.0) remain active for at least two weeks at room temperature. The solution retains activity after 5 freeze-thaw cycles.\u003c\/p\u003e\n\n\u003cp\u003eAnalysis Note\u003cbr\u003e\nThe RZ (Reinheitszahl) is the absorbance ratio A403\/A275 determined at 0.5-1.0 mg\/ml in deionized water. It is a measure of hemin content, not enzymatic activity. Even preparations with high RZ may have low enzymatic activity.\u003cbr\u003e\nThis product is assayed using ABTS for easy comparison to other suppliers′ unit: approx. 1,000 units per mg solid\u003c\/p\u003e\n\n\u003cp\u003eOther Notes\u003cbr\u003e\nOne ABTS unit will oxidize 1 μmole of ABTS per minute at 25 °C at pH 5.0\u003cbr\u003e\nOne pyrogallol unit will form 1.0 mg purpurogallin from pyrogallol in 20 sec at pH 6.0 at 20 °C.\u003cbr\u003e\nSimilar to P8375\u003c\/p\u003e","brand":"Millipore Sigma","offers":[{"title":"Default Title","offer_id":43042844049467,"sku":"P6782-5MG","price":104.25,"currency_code":"USD","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0606\/5641\/8875\/files\/P6782-10MG_5b36055e-15a9-4129-80ea-0cb65bc4e68e.png?v=1764188017"},{"product_id":"millipore-peroxidase-horseradish-type6a-10mg","title":"Peroxidase from horseradish  Type VI-A - 10MG","description":"\u003cp\u003ePeroxidase from horseradish - 10MG\u003cbr\u003e\nType VI-A, essentially salt-free, lyophilized powder, 950-2000 units\/mg solid (using ABTS), ≥250 units\/mg solid (using pyrogallol)\u003c\/p\u003e\n\n\u003cp\u003eSynonym(s): Donor:hydrogen-peroxide oxidoreductase, Horseradish peroxidase\u003c\/p\u003e\n\n\u003cp\u003eGeneral description\u003cbr\u003e\nHorseradish peroxidase is isolated from horseradish roots (Amoracia rusticana) and belongs to the ferroprotoporphyrin group of peroxidases. HRP is a single chain polypeptide containing four disulfide bridges. It is a glycoprotein containing 18% carbohydrate. The carbohydrate composition consists of galactose, arabinose, xylose, fucose, mannose, mannosamine, and galactosamine depending upon the specific isozyme. Its molecular weight (~44 kDa) includes the polypeptide chain (33,890 Daltons), hemin plus Ca2+ (~700 Daltons), and carbohydrate (~9,400 Daltons). At least seven isozymes of HRP exist. The isoelectric point for horseradish peroxidase isozymes ranges from 3.0 - 9.0.\u003c\/p\u003e\n\n\u003cp\u003eApplication\u003cbr\u003e\nHorseradish peroxidase (HRP) is isolated from horseradish roots (Amoracia rusticana). It is used in biochemistry applications such as western blots, ELISA and Immunohistochemistry. Horseradish peroxidase is used to amplify a weak signal and increase detectability of a target molecule, such as a protein. Product P6782 is type VI-A and it is essentially a salt-free, lyophilized powder. It is used to quantify cholesterol and cholesterol esters[1] and to study in vitro lipid deposition on hydrogel and silicone hydrogel contact lenses[2].\u003c\/p\u003e\n\n\u003cp\u003eThe enzyme from Sigma has been used in the development of rapid and sensitive galactose oxidase-peroxidase biosensor for galactose detection with prolonged stability.[3] It has been used as a component of a media (MRS agar) plate containing 3,3′,5,5′-tetramethylbenzidine (TMB) for the growth of Lactobacillus sp. TMB acts as a chromogenic substrate of peroxidase. Peroxidase generates O2 from H2O2 produced by the lactobacilli, and the TMB stains the colonies blue in the presence of O2. Thus, after 48 hours of incubation under 5% CO2 in air, the colonies that produce H2O2 on MRS agar appear dark blue. H2O2 nonproducers are colorless.[4] It has been used to study the stabilization effect of polyvinyl alcohol on horseradish peroxidase.[5] It is also used for the determination of glucose[6] and peroxides[7] in solution.\u003c\/p\u003e\n\n\u003cp\u003eBiochem\/physiol Actions\u003cbr\u003e\nHRP readily combines with hydrogen peroxide (H2O2) and the resultant [HRP-H2O2] complex can oxidize a wide variety of hydrogen donors. The optimal pH is 6.0-6.5 and the enzyme is most stable in the pH range of 5.0-9.0. HRP can be conjugated to antibodies by several different methods that include the use of glutaraldehyde, periodate oxidation, disulfide bonds, and also via amino and thiol directed cross-linkers. It is smaller and more stable than the enzyme labels, β-galactosidase and alkaline phosphatase. Hence, it is the most desired label. Also, its glycosylation leads to lower non-specific binding.[8] Sodium azide, cyanide, L-cystine, dichromate, ethylenethiourea, hydroxylamine, sulfide, vanadate, p-aminobenzoic acid, as well as Cd2+, Co2+, Cu2+, Fe3+, Mn2+, Ni2+, and Pb2+ ions are found to inhibit the enzyme activity.[9]\u003c\/p\u003e\n\n\u003cp\u003eWhen incubated with a substrate, horseradish peroxidase produces a coloured, fluorimetric, or luminescent derivative of the labeled molecule, allowing quantification. Horseradish peroxidase has been shown to slightly reduce the level of inhibition in a cydAB mutant.\u003c\/p\u003e\n\n\u003cp\u003ePackaging\u003cbr\u003e\nPackaged in mg solid\u003c\/p\u003e\n\n\u003cp\u003ePreparation Note\u003cbr\u003e\nSolutions of this product at 1 mg\/mL in 0.1 M phosphate buffer (pH 6.0) remain active for at least two weeks at room temperature. The solution retains activity after 5 freeze-thaw cycles.\u003c\/p\u003e\n\n\u003cp\u003eAnalysis Note\u003cbr\u003e\nThe RZ (Reinheitszahl) is the absorbance ratio A403\/A275 determined at 0.5-1.0 mg\/ml in deionized water. It is a measure of hemin content, not enzymatic activity. Even preparations with high RZ may have low enzymatic activity.\u003cbr\u003e\nThis product is assayed using ABTS for easy comparison to other suppliers′ unit: approx. 1,000 units per mg solid\u003c\/p\u003e\n\n\u003cp\u003eOther Notes\u003cbr\u003e\nOne ABTS unit will oxidize 1 μmole of ABTS per minute at 25 °C at pH 5.0\u003cbr\u003e\nOne pyrogallol unit will form 1.0 mg purpurogallin from pyrogallol in 20 sec at pH 6.0 at 20 °C.\u003cbr\u003e\nSimilar to P8375\u003c\/p\u003e","brand":"Millipore Sigma","offers":[{"title":"Default Title","offer_id":43042844147771,"sku":"P6782-10MG","price":198.75,"currency_code":"USD","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0606\/5641\/8875\/files\/P6782-10MG_b350c656-cbb0-483a-8c0e-0940d9f4da19.png?v=1764188018"},{"product_id":"millipore-peroxidase-horseradish-type6a-25mg","title":"Peroxidase from horseradish  Type VI-A- 25MG","description":"\u003cp\u003ePeroxidase from horseradish - 25MG\u003cbr\u003e\nType VI-A, essentially salt-free, lyophilized powder, 950-2000 units\/mg solid (using ABTS), ≥250 units\/mg solid (using pyrogallol)\u003c\/p\u003e\n\n\u003cp\u003eSynonym(s): Donor:hydrogen-peroxide oxidoreductase, Horseradish peroxidase\u003c\/p\u003e\n\n\u003cp\u003eGeneral description\u003cbr\u003e\nHorseradish peroxidase is isolated from horseradish roots (Amoracia rusticana) and belongs to the ferroprotoporphyrin group of peroxidases. HRP is a single chain polypeptide containing four disulfide bridges. It is a glycoprotein containing 18% carbohydrate. The carbohydrate composition consists of galactose, arabinose, xylose, fucose, mannose, mannosamine, and galactosamine depending upon the specific isozyme. Its molecular weight (~44 kDa) includes the polypeptide chain (33,890 Daltons), hemin plus Ca2+ (~700 Daltons), and carbohydrate (~9,400 Daltons). At least seven isozymes of HRP exist. The isoelectric point for horseradish peroxidase isozymes ranges from 3.0 - 9.0.\u003c\/p\u003e\n\n\u003cp\u003eApplication\u003cbr\u003e\nHorseradish peroxidase (HRP) is isolated from horseradish roots (Amoracia rusticana). It is used in biochemistry applications such as western blots, ELISA and Immunohistochemistry. Horseradish peroxidase is used to amplify a weak signal and increase detectability of a target molecule, such as a protein. Product P6782 is type VI-A and it is essentially a salt-free, lyophilized powder. It is used to quantify cholesterol and cholesterol esters[1] and to study in vitro lipid deposition on hydrogel and silicone hydrogel contact lenses[2].\u003c\/p\u003e\n\n\u003cp\u003eThe enzyme from Sigma has been used in the development of rapid and sensitive galactose oxidase-peroxidase biosensor for galactose detection with prolonged stability.[3] It has been used as a component of a media (MRS agar) plate containing 3,3′,5,5′-tetramethylbenzidine (TMB) for the growth of Lactobacillus sp. TMB acts as a chromogenic substrate of peroxidase. Peroxidase generates O2 from H2O2 produced by the lactobacilli, and the TMB stains the colonies blue in the presence of O2. Thus, after 48 hours of incubation under 5% CO2 in air, the colonies that produce H2O2 on MRS agar appear dark blue. H2O2 nonproducers are colorless.[4] It has been used to study the stabilization effect of polyvinyl alcohol on horseradish peroxidase.[5] It is also used for the determination of glucose[6] and peroxides[7] in solution.\u003c\/p\u003e\n\n\u003cp\u003eBiochem\/physiol Actions\u003cbr\u003e\nHRP readily combines with hydrogen peroxide (H2O2) and the resultant [HRP-H2O2] complex can oxidize a wide variety of hydrogen donors. The optimal pH is 6.0-6.5 and the enzyme is most stable in the pH range of 5.0-9.0. HRP can be conjugated to antibodies by several different methods that include the use of glutaraldehyde, periodate oxidation, disulfide bonds, and also via amino and thiol directed cross-linkers. It is smaller and more stable than the enzyme labels, β-galactosidase and alkaline phosphatase. Hence, it is the most desired label. Also, its glycosylation leads to lower non-specific binding.[8] Sodium azide, cyanide, L-cystine, dichromate, ethylenethiourea, hydroxylamine, sulfide, vanadate, p-aminobenzoic acid, as well as Cd2+, Co2+, Cu2+, Fe3+, Mn2+, Ni2+, and Pb2+ ions are found to inhibit the enzyme activity.[9]\u003c\/p\u003e\n\n\u003cp\u003eWhen incubated with a substrate, horseradish peroxidase produces a coloured, fluorimetric, or luminescent derivative of the labeled molecule, allowing quantification. Horseradish peroxidase has been shown to slightly reduce the level of inhibition in a cydAB mutant.\u003c\/p\u003e\n\n\u003cp\u003ePackaging\u003cbr\u003e\nPackaged in mg solid\u003c\/p\u003e\n\n\u003cp\u003ePreparation Note\u003cbr\u003e\nSolutions of this product at 1 mg\/mL in 0.1 M phosphate buffer (pH 6.0) remain active for at least two weeks at room temperature. The solution retains activity after 5 freeze-thaw cycles.\u003c\/p\u003e\n\n\u003cp\u003eAnalysis Note\u003cbr\u003e\nThe RZ (Reinheitszahl) is the absorbance ratio A403\/A275 determined at 0.5-1.0 mg\/ml in deionized water. It is a measure of hemin content, not enzymatic activity. Even preparations with high RZ may have low enzymatic activity.\u003cbr\u003e\nThis product is assayed using ABTS for easy comparison to other suppliers′ unit: approx. 1,000 units per mg solid\u003c\/p\u003e\n\n\u003cp\u003eOther Notes\u003cbr\u003e\nOne ABTS unit will oxidize 1 μmole of ABTS per minute at 25 °C at pH 5.0\u003cbr\u003e\nOne pyrogallol unit will form 1.0 mg purpurogallin from pyrogallol in 20 sec at pH 6.0 at 20 °C.\u003cbr\u003e\nSimilar to P8375\u003c\/p\u003e","brand":"Millipore Sigma","offers":[{"title":"Default Title","offer_id":43042844246075,"sku":"P6782-25MG","price":323.75,"currency_code":"USD","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0606\/5641\/8875\/files\/P6782-25MG_07d36c11-a168-427d-8090-51d781d7f59e.png?v=1764188018"},{"product_id":"millipore-peroxidase-horseradish-type6a-50mg","title":"Peroxidase from horseradish  Type VI-A - 50MG","description":"\u003cp\u003ePeroxidase from horseradish - 50MG\u003cbr\u003e\nType VI-A, essentially salt-free, lyophilized powder, 950-2000 units\/mg solid (using ABTS), ≥250 units\/mg solid (using pyrogallol)\u003c\/p\u003e\n\n\u003cp\u003eSynonym(s): Donor:hydrogen-peroxide oxidoreductase, Horseradish peroxidase\u003c\/p\u003e\n\n\u003cp\u003eGeneral description\u003cbr\u003e\nHorseradish peroxidase is isolated from horseradish roots (Amoracia rusticana) and belongs to the ferroprotoporphyrin group of peroxidases. HRP is a single chain polypeptide containing four disulfide bridges. It is a glycoprotein containing 18% carbohydrate. The carbohydrate composition consists of galactose, arabinose, xylose, fucose, mannose, mannosamine, and galactosamine depending upon the specific isozyme. Its molecular weight (~44 kDa) includes the polypeptide chain (33,890 Daltons), hemin plus Ca2+ (~700 Daltons), and carbohydrate (~9,400 Daltons). At least seven isozymes of HRP exist. The isoelectric point for horseradish peroxidase isozymes ranges from 3.0 - 9.0.\u003c\/p\u003e\n\n\u003cp\u003eApplication\u003cbr\u003e\nHorseradish peroxidase (HRP) is isolated from horseradish roots (Amoracia rusticana). It is used in biochemistry applications such as western blots, ELISA and Immunohistochemistry. Horseradish peroxidase is used to amplify a weak signal and increase detectability of a target molecule, such as a protein. Product P6782 is type VI-A and it is essentially a salt-free, lyophilized powder. It is used to quantify cholesterol and cholesterol esters[1] and to study in vitro lipid deposition on hydrogel and silicone hydrogel contact lenses[2].\u003c\/p\u003e\n\n\u003cp\u003eThe enzyme from Sigma has been used in the development of rapid and sensitive galactose oxidase-peroxidase biosensor for galactose detection with prolonged stability.[3] It has been used as a component of a media (MRS agar) plate containing 3,3′,5,5′-tetramethylbenzidine (TMB) for the growth of Lactobacillus sp. TMB acts as a chromogenic substrate of peroxidase. Peroxidase generates O2 from H2O2 produced by the lactobacilli, and the TMB stains the colonies blue in the presence of O2. Thus, after 48 hours of incubation under 5% CO2 in air, the colonies that produce H2O2 on MRS agar appear dark blue. H2O2 nonproducers are colorless.[4] It has been used to study the stabilization effect of polyvinyl alcohol on horseradish peroxidase.[5] It is also used for the determination of glucose[6] and peroxides[7] in solution.\u003c\/p\u003e\n\n\u003cp\u003eBiochem\/physiol Actions\u003cbr\u003e\nHRP readily combines with hydrogen peroxide (H2O2) and the resultant [HRP-H2O2] complex can oxidize a wide variety of hydrogen donors. The optimal pH is 6.0-6.5 and the enzyme is most stable in the pH range of 5.0-9.0. HRP can be conjugated to antibodies by several different methods that include the use of glutaraldehyde, periodate oxidation, disulfide bonds, and also via amino and thiol directed cross-linkers. It is smaller and more stable than the enzyme labels, β-galactosidase and alkaline phosphatase. Hence, it is the most desired label. Also, its glycosylation leads to lower non-specific binding.[8] Sodium azide, cyanide, L-cystine, dichromate, ethylenethiourea, hydroxylamine, sulfide, vanadate, p-aminobenzoic acid, as well as Cd2+, Co2+, Cu2+, Fe3+, Mn2+, Ni2+, and Pb2+ ions are found to inhibit the enzyme activity.[9]\u003c\/p\u003e\n\n\u003cp\u003eWhen incubated with a substrate, horseradish peroxidase produces a coloured, fluorimetric, or luminescent derivative of the labeled molecule, allowing quantification. Horseradish peroxidase has been shown to slightly reduce the level of inhibition in a cydAB mutant.\u003c\/p\u003e\n\n\u003cp\u003ePackaging\u003cbr\u003e\nPackaged in mg solid\u003c\/p\u003e\n\n\u003cp\u003ePreparation Note\u003cbr\u003e\nSolutions of this product at 1 mg\/mL in 0.1 M phosphate buffer (pH 6.0) remain active for at least two weeks at room temperature. The solution retains activity after 5 freeze-thaw cycles.\u003c\/p\u003e\n\n\u003cp\u003eAnalysis Note\u003cbr\u003e\nThe RZ (Reinheitszahl) is the absorbance ratio A403\/A275 determined at 0.5-1.0 mg\/ml in deionized water. It is a measure of hemin content, not enzymatic activity. Even preparations with high RZ may have low enzymatic activity.\u003cbr\u003e\nThis product is assayed using ABTS for easy comparison to other suppliers′ unit: approx. 1,000 units per mg solid\u003c\/p\u003e\n\n\u003cp\u003eOther Notes\u003cbr\u003e\nOne ABTS unit will oxidize 1 μmole of ABTS per minute at 25 °C at pH 5.0\u003cbr\u003e\nOne pyrogallol unit will form 1.0 mg purpurogallin from pyrogallol in 20 sec at pH 6.0 at 20 °C.\u003cbr\u003e\nSimilar to P8375\u003c\/p\u003e","brand":"Millipore Sigma","offers":[{"title":"Default Title","offer_id":43042844311611,"sku":"P6782-50MG","price":561.25,"currency_code":"USD","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0606\/5641\/8875\/files\/P6782-50MG_d6d0f62d-d9ef-4fbd-9693-bfc80b8460ff.png?v=1764188019"},{"product_id":"millipore-peroxidase-horseradish-type6a-100mg","title":"Peroxidase from horseradish Type VI-A - 100MG","description":"\u003cp\u003ePeroxidase from horseradish - 100MG\u003cbr\u003e\nType VI-A, essentially salt-free, lyophilized powder, 950-2000 units\/mg solid (using ABTS), ≥250 units\/mg solid (using pyrogallol)\u003c\/p\u003e\n\n\u003cp\u003eSynonym(s): Donor:hydrogen-peroxide oxidoreductase, Horseradish peroxidase\u003c\/p\u003e\n\n\u003cp\u003eGeneral description\u003cbr\u003e\nHorseradish peroxidase is isolated from horseradish roots (Amoracia rusticana) and belongs to the ferroprotoporphyrin group of peroxidases. HRP is a single chain polypeptide containing four disulfide bridges. It is a glycoprotein containing 18% carbohydrate. The carbohydrate composition consists of galactose, arabinose, xylose, fucose, mannose, mannosamine, and galactosamine depending upon the specific isozyme. Its molecular weight (~44 kDa) includes the polypeptide chain (33,890 Daltons), hemin plus Ca2+ (~700 Daltons), and carbohydrate (~9,400 Daltons). At least seven isozymes of HRP exist. The isoelectric point for horseradish peroxidase isozymes ranges from 3.0 - 9.0.\u003c\/p\u003e\n\n\u003cp\u003eApplication\u003cbr\u003e\nHorseradish peroxidase (HRP) is isolated from horseradish roots (Amoracia rusticana). It is used in biochemistry applications such as western blots, ELISA and Immunohistochemistry. Horseradish peroxidase is used to amplify a weak signal and increase detectability of a target molecule, such as a protein. Product P6782 is type VI-A and it is essentially a salt-free, lyophilized powder. It is used to quantify cholesterol and cholesterol esters[1] and to study in vitro lipid deposition on hydrogel and silicone hydrogel contact lenses[2].\u003c\/p\u003e\n\n\u003cp\u003eThe enzyme from Sigma has been used in the development of rapid and sensitive galactose oxidase-peroxidase biosensor for galactose detection with prolonged stability.[3] It has been used as a component of a media (MRS agar) plate containing 3,3′,5,5′-tetramethylbenzidine (TMB) for the growth of Lactobacillus sp. TMB acts as a chromogenic substrate of peroxidase. Peroxidase generates O2 from H2O2 produced by the lactobacilli, and the TMB stains the colonies blue in the presence of O2. Thus, after 48 hours of incubation under 5% CO2 in air, the colonies that produce H2O2 on MRS agar appear dark blue. H2O2 nonproducers are colorless.[4] It has been used to study the stabilization effect of polyvinyl alcohol on horseradish peroxidase.[5] It is also used for the determination of glucose[6] and peroxides[7] in solution.\u003c\/p\u003e\n\n\u003cp\u003eBiochem\/physiol Actions\u003cbr\u003e\nHRP readily combines with hydrogen peroxide (H2O2) and the resultant [HRP-H2O2] complex can oxidize a wide variety of hydrogen donors. The optimal pH is 6.0-6.5 and the enzyme is most stable in the pH range of 5.0-9.0. HRP can be conjugated to antibodies by several different methods that include the use of glutaraldehyde, periodate oxidation, disulfide bonds, and also via amino and thiol directed cross-linkers. It is smaller and more stable than the enzyme labels, β-galactosidase and alkaline phosphatase. Hence, it is the most desired label. Also, its glycosylation leads to lower non-specific binding.[8] Sodium azide, cyanide, L-cystine, dichromate, ethylenethiourea, hydroxylamine, sulfide, vanadate, p-aminobenzoic acid, as well as Cd2+, Co2+, Cu2+, Fe3+, Mn2+, Ni2+, and Pb2+ ions are found to inhibit the enzyme activity.[9]\u003c\/p\u003e\n\n\u003cp\u003eWhen incubated with a substrate, horseradish peroxidase produces a coloured, fluorimetric, or luminescent derivative of the labeled molecule, allowing quantification. Horseradish peroxidase has been shown to slightly reduce the level of inhibition in a cydAB mutant.\u003c\/p\u003e\n\n\u003cp\u003ePackaging\u003cbr\u003e\nPackaged in mg solid\u003c\/p\u003e\n\n\u003cp\u003ePreparation Note\u003cbr\u003e\nSolutions of this product at 1 mg\/mL in 0.1 M phosphate buffer (pH 6.0) remain active for at least two weeks at room temperature. The solution retains activity after 5 freeze-thaw cycles.\u003c\/p\u003e\n\n\u003cp\u003eAnalysis Note\u003cbr\u003e\nThe RZ (Reinheitszahl) is the absorbance ratio A403\/A275 determined at 0.5-1.0 mg\/ml in deionized water. It is a measure of hemin content, not enzymatic activity. Even preparations with high RZ may have low enzymatic activity.\u003cbr\u003e\nThis product is assayed using ABTS for easy comparison to other suppliers′ unit: approx. 1,000 units per mg solid\u003c\/p\u003e\n\n\u003cp\u003eOther Notes\u003cbr\u003e\nOne ABTS unit will oxidize 1 μmole of ABTS per minute at 25 °C at pH 5.0\u003cbr\u003e\nOne pyrogallol unit will form 1.0 mg purpurogallin from pyrogallol in 20 sec at pH 6.0 at 20 °C.\u003cbr\u003e\nSimilar to P8375\u003c\/p\u003e","brand":"Millipore Sigma","offers":[{"title":"Default Title","offer_id":43042844442683,"sku":"P6782-100MG","price":963.75,"currency_code":"USD","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0606\/5641\/8875\/files\/P6782-100MG_a454b206-bdb9-42bc-818a-59d28b47c806.png?v=1764188020"},{"product_id":"millipore-peroxidase-horseradish-type2-5mg","title":"Peroxidase from horseradish Type II - 5MG","description":"\u003cp\u003ePeroxidase from horseradish\u003cbr\u003e\nType VI-A, essentially salt-free, lyophilized powder, 950-2000 units\/mg solid (using ABTS), ≥250 units\/mg solid (using pyrogallol)\u003c\/p\u003e\n\n\u003cp\u003eSynonym(s):\u003cbr\u003e\nDonor:hydrogen-peroxide oxidoreductase, Horseradish peroxidase\u003c\/p\u003e\n\n\u003cp\u003eGeneral description\u003cbr\u003e\nHorseradish peroxidase is isolated from horseradish roots (Amoracia rusticana) and belongs to the ferroprotoporphyrin group of peroxidases. HRP is a single chain polypeptide containing four disulfide bridges. It is a glycoprotein containing 18% carbohydrate. The carbohydrate composition consists of galactose, arabinose, xylose, fucose, mannose, mannosamine, and galactosamine depending upon the specific isozyme. Its molecular weight (~44 kDa) includes the polypeptide chain (33,890 Daltons), hemin plus Ca2+ (~700 Daltons), and carbohydrate (~9,400 Daltons). At least seven isozymes of HRP exist. The isoelectric point for horseradish peroxidase isozymes ranges from 3.0 - 9.0.\u003c\/p\u003e\n\n\u003cp\u003eApplication\u003cbr\u003e\nHorseradish peroxidase (HRP) is isolated from horseradish roots (Amoracia rusticana). It is used in biochemistry applications such as western blots, ELISA and Immunohistochemistry. Horseradish peroxidase is used to amplify a weak signal and increase detectability of a target molecule, such as a protein. Product P6782 is type VI-A and it is essentially a salt-free, lyophilized powder. It is used to quantify cholesterol and cholesterol esters[1] and to study in vitro lipid deposition on hydrogel and silicone hydrogel contact lenses[2].\u003c\/p\u003e\n\n\u003cp\u003eThe enzyme from Sigma has been used in the development of rapid and sensitive galactose oxidase-peroxidase biosensor for galactose detection with prolonged stability.[3] It has been used as a component of a media (MRS agar) plate containing 3,3′,5,5′-tetramethylbenzidine (TMB) for the growth of Lactobacillus sp. TMB acts as a chromogenic substrate of peroxidase. Peroxidase generates O2 from H2O2 produced by the lactobacilli, and the TMB stains the colonies blue in the presence of O2. Thus, after 48 hours of incubation under 5% CO2 in air, the colonies that produce H2O2 on MRS agar appear dark blue. H2O2 nonproducers are colorless.[4] It has been used to study the stabilization effect of polyvinyl alcohol on horseradish peroxidase.[5] It is also used for the determination of glucose[6] and peroxides[7] in solution.\u003c\/p\u003e\n\n\u003cp\u003eBiochem\/physiol Actions\u003cbr\u003e\nHRP readily combines with hydrogen peroxide (H2O2) and the resultant [HRP-H2O2] complex can oxidize a wide variety of hydrogen donors. The optimal pH is 6.0-6.5 and the enzyme is most stable in the pH range of 5.0-9.0. HRP can be conjugated to antibodies by several different methods that include the use of glutaraldehyde, periodate oxidation, disulfide bonds, and also via amino and thiol directed cross-linkers. It is smaller and more stable than the enzyme labels, β-galactosidase and alkaline phosphatase. Hence, it is the most desired label. Also, its glycosylation leads to lower non-specific binding.[8] Sodium azide, cyanide, L-cystine, dichromate, ethylenethiourea, hydroxylamine, sulfide, vanadate, p-aminobenzoic acid, as well as Cd2+, Co2+, Cu2+, Fe3+, Mn2+, Ni2+, and Pb2+ ions are found to inhibit the enzyme activity.[9]\u003c\/p\u003e\n\n\u003cp\u003eWhen incubated with a substrate, horseradish peroxidase produces a coloured, fluorimetric, or luminescent derivative of the labeled molecule, allowing quantification. Horseradish peroxidase has been shown to slightly reduce the level of inhibition in a cydAB mutant.\u003c\/p\u003e\n\n\u003cp\u003ePackaging\u003cbr\u003e\nPackaged in mg solid\u003c\/p\u003e\n\n\u003cp\u003ePreparation Note\u003cbr\u003e\nSolutions of this product at 1 mg\/mL in 0.1 M phosphate buffer (pH 6.0) remain active for at least two weeks at room temperature. The solution retains activity after 5 freeze-thaw cycles.\u003c\/p\u003e\n\n\u003cp\u003eAnalysis Note\u003cbr\u003e\nThe RZ (Reinheitszahl) is the absorbance ratio A403\/A275 determined at 0.5-1.0 mg\/ml in deionized water. It is a measure of hemin content, not enzymatic activity. Even preparations with high RZ may have low enzymatic activity.\u003cbr\u003e\nThis product is assayed using ABTS for easy comparison to other suppliers′ unit: approx. 1,000 units per mg solid\u003c\/p\u003e\n\n\u003cp\u003eOther Notes\u003cbr\u003e\nOne ABTS unit will oxidize 1 μmole of ABTS per minute at 25 °C at pH 5.0\u003cbr\u003e\nOne pyrogallol unit will form 1.0 mg purpurogallin from pyrogallol in 20 sec at pH 6.0 at 20 °C.\u003cbr\u003e\nSimilar to P8375\u003c\/p\u003e","brand":"Millipore Sigma","offers":[{"title":"Default Title","offer_id":43042844508219,"sku":"P8250-5KU","price":105.0,"currency_code":"USD","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0606\/5641\/8875\/files\/P8250-5KU_ba3a9d3a-473d-483b-a05b-10b440ffde4e.png?v=1764188021"},{"product_id":"millipore-peroxidase-horseradish-type2-25mg","title":"Peroxidase from horseradish Type II - 25MG","description":"\u003cp\u003ePeroxidase from horseradish\u003cbr\u003e\nType VI-A, essentially salt-free, lyophilized powder, 950-2000 units\/mg solid (using ABTS), ≥250 units\/mg solid (using pyrogallol)\u003c\/p\u003e\n\n\u003cp\u003eSynonym(s):\u003cbr\u003e\nDonor:hydrogen-peroxide oxidoreductase, Horseradish peroxidase\u003c\/p\u003e\n\n\u003cp\u003eGeneral description\u003cbr\u003e\nHorseradish peroxidase is isolated from horseradish roots (Amoracia rusticana) and belongs to the ferroprotoporphyrin group of peroxidases. HRP is a single chain polypeptide containing four disulfide bridges. It is a glycoprotein containing 18% carbohydrate. The carbohydrate composition consists of galactose, arabinose, xylose, fucose, mannose, mannosamine, and galactosamine depending upon the specific isozyme. Its molecular weight (~44 kDa) includes the polypeptide chain (33,890 Daltons), hemin plus Ca2+ (~700 Daltons), and carbohydrate (~9,400 Daltons). At least seven isozymes of HRP exist. The isoelectric point for horseradish peroxidase isozymes ranges from 3.0 - 9.0.\u003c\/p\u003e\n\n\u003cp\u003eApplication\u003cbr\u003e\nHorseradish peroxidase (HRP) is isolated from horseradish roots (Amoracia rusticana). It is used in biochemistry applications such as western blots, ELISA and Immunohistochemistry. Horseradish peroxidase is used to amplify a weak signal and increase detectability of a target molecule, such as a protein. Product P6782 is type VI-A and it is essentially a salt-free, lyophilized powder. It is used to quantify cholesterol and cholesterol esters[1] and to study in vitro lipid deposition on hydrogel and silicone hydrogel contact lenses[2].\u003c\/p\u003e\n\n\u003cp\u003eThe enzyme from Sigma has been used in the development of rapid and sensitive galactose oxidase-peroxidase biosensor for galactose detection with prolonged stability.[3] It has been used as a component of a media (MRS agar) plate containing 3,3′,5,5′-tetramethylbenzidine (TMB) for the growth of Lactobacillus sp. TMB acts as a chromogenic substrate of peroxidase. Peroxidase generates O2 from H2O2 produced by the lactobacilli, and the TMB stains the colonies blue in the presence of O2. Thus, after 48 hours of incubation under 5% CO2 in air, the colonies that produce H2O2 on MRS agar appear dark blue. H2O2 nonproducers are colorless.[4] It has been used to study the stabilization effect of polyvinyl alcohol on horseradish peroxidase.[5] It is also used for the determination of glucose[6] and peroxides[7] in solution.\u003c\/p\u003e\n\n\u003cp\u003eBiochem\/physiol Actions\u003cbr\u003e\nHRP readily combines with hydrogen peroxide (H2O2) and the resultant [HRP-H2O2] complex can oxidize a wide variety of hydrogen donors. The optimal pH is 6.0-6.5 and the enzyme is most stable in the pH range of 5.0-9.0. HRP can be conjugated to antibodies by several different methods that include the use of glutaraldehyde, periodate oxidation, disulfide bonds, and also via amino and thiol directed cross-linkers. It is smaller and more stable than the enzyme labels, β-galactosidase and alkaline phosphatase. Hence, it is the most desired label. Also, its glycosylation leads to lower non-specific binding.[8] Sodium azide, cyanide, L-cystine, dichromate, ethylenethiourea, hydroxylamine, sulfide, vanadate, p-aminobenzoic acid, as well as Cd2+, Co2+, Cu2+, Fe3+, Mn2+, Ni2+, and Pb2+ ions are found to inhibit the enzyme activity.[9]\u003c\/p\u003e\n\n\u003cp\u003eWhen incubated with a substrate, horseradish peroxidase produces a coloured, fluorimetric, or luminescent derivative of the labeled molecule, allowing quantification. Horseradish peroxidase has been shown to slightly reduce the level of inhibition in a cydAB mutant.\u003c\/p\u003e\n\n\u003cp\u003ePackaging\u003cbr\u003e\nPackaged in mg solid\u003c\/p\u003e\n\n\u003cp\u003ePreparation Note\u003cbr\u003e\nSolutions of this product at 1 mg\/mL in 0.1 M phosphate buffer (pH 6.0) remain active for at least two weeks at room temperature. The solution retains activity after 5 freeze-thaw cycles.\u003c\/p\u003e\n\n\u003cp\u003eAnalysis Note\u003cbr\u003e\nThe RZ (Reinheitszahl) is the absorbance ratio A403\/A275 determined at 0.5-1.0 mg\/ml in deionized water. It is a measure of hemin content, not enzymatic activity. Even preparations with high RZ may have low enzymatic activity.\u003cbr\u003e\nThis product is assayed using ABTS for easy comparison to other suppliers′ unit: approx. 1,000 units per mg solid\u003c\/p\u003e\n\n\u003cp\u003eOther Notes\u003cbr\u003e\nOne ABTS unit will oxidize 1 μmole of ABTS per minute at 25 °C at pH 5.0\u003cbr\u003e\nOne pyrogallol unit will form 1.0 mg purpurogallin from pyrogallol in 20 sec at pH 6.0 at 20 °C.\u003cbr\u003e\nSimilar to P8375\u003c\/p\u003e","brand":"Millipore Sigma","offers":[{"title":"Default Title","offer_id":43042844639291,"sku":"P8250-25KU","price":346.25,"currency_code":"USD","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0606\/5641\/8875\/files\/P8250-25KU_b0545cec-1562-4625-a651-beb4f24e124c.png?v=1764188021"},{"product_id":"millipore-peroxidase-horseradish-type2-50mg","title":"Peroxidase from horseradish Type II - 50MG","description":"\u003cp\u003ePeroxidase from horseradish\u003cbr\u003e\nType VI-A, essentially salt-free, lyophilized powder, 950-2000 units\/mg solid (using ABTS), ≥250 units\/mg solid (using pyrogallol)\u003c\/p\u003e\n\n\u003cp\u003eSynonym(s):\u003cbr\u003e\nDonor:hydrogen-peroxide oxidoreductase, Horseradish peroxidase\u003c\/p\u003e\n\n\u003cp\u003eGeneral description\u003cbr\u003e\nHorseradish peroxidase is isolated from horseradish roots (Amoracia rusticana) and belongs to the ferroprotoporphyrin group of peroxidases. HRP is a single chain polypeptide containing four disulfide bridges. It is a glycoprotein containing 18% carbohydrate. The carbohydrate composition consists of galactose, arabinose, xylose, fucose, mannose, mannosamine, and galactosamine depending upon the specific isozyme. Its molecular weight (~44 kDa) includes the polypeptide chain (33,890 Daltons), hemin plus Ca2+ (~700 Daltons), and carbohydrate (~9,400 Daltons). At least seven isozymes of HRP exist. The isoelectric point for horseradish peroxidase isozymes ranges from 3.0 - 9.0.\u003c\/p\u003e\n\n\u003cp\u003eApplication\u003cbr\u003e\nHorseradish peroxidase (HRP) is isolated from horseradish roots (Amoracia rusticana). It is used in biochemistry applications such as western blots, ELISA and Immunohistochemistry. Horseradish peroxidase is used to amplify a weak signal and increase detectability of a target molecule, such as a protein. Product P6782 is type VI-A and it is essentially a salt-free, lyophilized powder. It is used to quantify cholesterol and cholesterol esters[1] and to study in vitro lipid deposition on hydrogel and silicone hydrogel contact lenses[2].\u003c\/p\u003e\n\n\u003cp\u003eThe enzyme from Sigma has been used in the development of rapid and sensitive galactose oxidase-peroxidase biosensor for galactose detection with prolonged stability.[3] It has been used as a component of a media (MRS agar) plate containing 3,3′,5,5′-tetramethylbenzidine (TMB) for the growth of Lactobacillus sp. TMB acts as a chromogenic substrate of peroxidase. Peroxidase generates O2 from H2O2 produced by the lactobacilli, and the TMB stains the colonies blue in the presence of O2. Thus, after 48 hours of incubation under 5% CO2 in air, the colonies that produce H2O2 on MRS agar appear dark blue. H2O2 nonproducers are colorless.[4] It has been used to study the stabilization effect of polyvinyl alcohol on horseradish peroxidase.[5] It is also used for the determination of glucose[6] and peroxides[7] in solution.\u003c\/p\u003e\n\n\u003cp\u003eBiochem\/physiol Actions\u003cbr\u003e\nHRP readily combines with hydrogen peroxide (H2O2) and the resultant [HRP-H2O2] complex can oxidize a wide variety of hydrogen donors. The optimal pH is 6.0-6.5 and the enzyme is most stable in the pH range of 5.0-9.0. HRP can be conjugated to antibodies by several different methods that include the use of glutaraldehyde, periodate oxidation, disulfide bonds, and also via amino and thiol directed cross-linkers. It is smaller and more stable than the enzyme labels, β-galactosidase and alkaline phosphatase. Hence, it is the most desired label. Also, its glycosylation leads to lower non-specific binding.[8] Sodium azide, cyanide, L-cystine, dichromate, ethylenethiourea, hydroxylamine, sulfide, vanadate, p-aminobenzoic acid, as well as Cd2+, Co2+, Cu2+, Fe3+, Mn2+, Ni2+, and Pb2+ ions are found to inhibit the enzyme activity.[9]\u003c\/p\u003e\n\n\u003cp\u003eWhen incubated with a substrate, horseradish peroxidase produces a coloured, fluorimetric, or luminescent derivative of the labeled molecule, allowing quantification. Horseradish peroxidase has been shown to slightly reduce the level of inhibition in a cydAB mutant.\u003c\/p\u003e\n\n\u003cp\u003ePackaging\u003cbr\u003e\nPackaged in mg solid\u003c\/p\u003e\n\n\u003cp\u003ePreparation Note\u003cbr\u003e\nSolutions of this product at 1 mg\/mL in 0.1 M phosphate buffer (pH 6.0) remain active for at least two weeks at room temperature. The solution retains activity after 5 freeze-thaw cycles.\u003c\/p\u003e\n\n\u003cp\u003eAnalysis Note\u003cbr\u003e\nThe RZ (Reinheitszahl) is the absorbance ratio A403\/A275 determined at 0.5-1.0 mg\/ml in deionized water. It is a measure of hemin content, not enzymatic activity. Even preparations with high RZ may have low enzymatic activity.\u003cbr\u003e\nThis product is assayed using ABTS for easy comparison to other suppliers′ unit: approx. 1,000 units per mg solid\u003c\/p\u003e\n\n\u003cp\u003eOther Notes\u003cbr\u003e\nOne ABTS unit will oxidize 1 μmole of ABTS per minute at 25 °C at pH 5.0\u003cbr\u003e\nOne pyrogallol unit will form 1.0 mg purpurogallin from pyrogallol in 20 sec at pH 6.0 at 20 °C.\u003cbr\u003e\nSimilar to P8375\u003c\/p\u003e","brand":"Millipore Sigma","offers":[{"title":"Default Title","offer_id":43042844770363,"sku":"P8250-50KU","price":486.25,"currency_code":"USD","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0606\/5641\/8875\/files\/P8250-50KU_3710d179-cf7a-4c3c-86a7-dbbd1bf310c8.png?v=1764188022"},{"product_id":"millipore-peroxidase-horseradish-type2-100mg","title":"Peroxidase from horseradish Type II - 100MG","description":"\u003cp\u003e\u003cstrong\u003ePeroxidase from horseradish\u003c\/strong\u003e\u003cbr\u003eType VI-A, essentially salt-free, lyophilized powder, 950-2000 units\/mg solid (using ABTS), ≥250 units\/mg solid (using pyrogallol)\u003c\/p\u003e\n\u003cp\u003eSynonym(s):\u003cbr\u003eDonor:hydrogen-peroxide oxidoreductase, Horseradish peroxidase\u003c\/p\u003e\n\u003cp\u003e\u003cstrong\u003eGeneral description\u003c\/strong\u003e\u003cbr\u003eHorseradish peroxidase is isolated from horseradish roots (Amoracia rusticana) and belongs to the ferroprotoporphyrin group of peroxidases. HRP is a single chain polypeptide containing four disulfide bridges. It is a glycoprotein containing 18% carbohydrate. The carbohydrate composition consists of galactose, arabinose, xylose, fucose, mannose, mannosamine, and galactosamine depending upon the specific isozyme. Its molecular weight (~44 kDa) includes the polypeptide chain (33,890 Daltons), hemin plus Ca2+ (~700 Daltons), and carbohydrate (~9,400 Daltons). At least seven isozymes of HRP exist. The isoelectric point for horseradish peroxidase isozymes ranges from 3.0 - 9.0.\u003c\/p\u003e\n\u003cp\u003e\u003cstrong\u003eApplication\u003c\/strong\u003e\u003cbr\u003eHorseradish peroxidase (HRP) is isolated from horseradish roots (Amoracia rusticana). It is used in biochemistry applications such as western blots, ELISA and Immunohistochemistry. Horseradish peroxidase is used to amplify a weak signal and increase detectability of a target molecule, such as a protein. Product P6782 is type VI-A and it is essentially a salt-free, lyophilized powder. It is used to quantify cholesterol and cholesterol esters[1] and to study in vitro lipid deposition on hydrogel and silicone hydrogel contact lenses[2].\u003c\/p\u003e\n\u003cp\u003eThe enzyme from Sigma has been used in the development of rapid and sensitive galactose oxidase-peroxidase biosensor for galactose detection with prolonged stability.[3] It has been used as a component of a media (MRS agar) plate containing 3,3′,5,5′-tetramethylbenzidine (TMB) for the growth of Lactobacillus sp. TMB acts as a chromogenic substrate of peroxidase. Peroxidase generates O2 from H2O2 produced by the lactobacilli, and the TMB stains the colonies blue in the presence of O2. Thus, after 48 hours of incubation under 5% CO2 in air, the colonies that produce H2O2 on MRS agar appear dark blue. H2O2 nonproducers are colorless.[4] It has been used to study the stabilization effect of polyvinyl alcohol on horseradish peroxidase.[5] It is also used for the determination of glucose[6] and peroxides[7] in solution.\u003c\/p\u003e\n\u003cp\u003e\u003cstrong\u003eBiochem\/physiol Actions\u003c\/strong\u003e\u003cbr\u003eHRP readily combines with hydrogen peroxide (H2O2) and the resultant [HRP-H2O2] complex can oxidize a wide variety of hydrogen donors. The optimal pH is 6.0-6.5 and the enzyme is most stable in the pH range of 5.0-9.0. HRP can be conjugated to antibodies by several different methods that include the use of glutaraldehyde, periodate oxidation, disulfide bonds, and also via amino and thiol directed cross-linkers. It is smaller and more stable than the enzyme labels, β-galactosidase and alkaline phosphatase. Hence, it is the most desired label. Also, its glycosylation leads to lower non-specific binding.[8] Sodium azide, cyanide, L-cystine, dichromate, ethylenethiourea, hydroxylamine, sulfide, vanadate, p-aminobenzoic acid, as well as Cd2+, Co2+, Cu2+, Fe3+, Mn2+, Ni2+, and Pb2+ ions are found to inhibit the enzyme activity.[9]\u003c\/p\u003e\n\u003cp\u003eWhen incubated with a substrate, horseradish peroxidase produces a coloured, fluorimetric, or luminescent derivative of the labeled molecule, allowing quantification. Horseradish peroxidase has been shown to slightly reduce the level of inhibition in a cydAB mutant.\u003c\/p\u003e\n\u003cp\u003e\u003cstrong\u003ePackaging\u003c\/strong\u003e\u003cbr\u003ePackaged in mg solid\u003c\/p\u003e\n\u003cp\u003e\u003cstrong\u003ePreparation Note\u003c\/strong\u003e\u003cbr\u003eSolutions of this product at 1 mg\/mL in 0.1 M phosphate buffer (pH 6.0) remain active for at least two weeks at room temperature. The solution retains activity after 5 freeze-thaw cycles.\u003c\/p\u003e\n\u003cp\u003e\u003cstrong\u003eAnalysis Note\u003c\/strong\u003e\u003cbr\u003eThe RZ (Reinheitszahl) is the absorbance ratio A403\/A275 determined at 0.5-1.0 mg\/ml in deionized water. It is a measure of hemin content, not enzymatic activity. Even preparations with high RZ may have low enzymatic activity.\u003cbr\u003eThis product is assayed using ABTS for easy comparison to other suppliers′ unit: approx. 1,000 units per mg solid\u003c\/p\u003e\n\u003cp\u003e\u003cstrong\u003eOther Notes\u003c\/strong\u003e\u003cbr\u003eOne ABTS unit will oxidize 1 μmole of ABTS per minute at 25 °C at pH 5.0\u003cbr\u003eOne pyrogallol unit will form 1.0 mg purpurogallin from pyrogallol in 20 sec at pH 6.0 at 20 °C.\u003cbr\u003eSimilar to P8375\u003c\/p\u003e","brand":"Millipore Sigma","offers":[{"title":"Default Title","offer_id":43042844868667,"sku":"P8250-100KU","price":847.5,"currency_code":"USD","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0606\/5641\/8875\/files\/P8250-100KU_4970d0b9-6863-4380-86d2-484bcac9857a.png?v=1764188023"},{"product_id":"millipore-peroxidase-horseradish-type2-200mg","title":"Peroxidase from horseradish Type II - 200MG","description":"\u003cp\u003e\u003cstrong\u003ePeroxidase from horseradish\u003c\/strong\u003e\u003cbr\u003eType VI-A, essentially salt-free, lyophilized powder, 950-2000 units\/mg solid (using ABTS), ≥250 units\/mg solid (using pyrogallol)\u003c\/p\u003e\n\u003cp\u003e\u003cstrong\u003eSynonym(s):\u003c\/strong\u003e\u003cbr\u003eDonor:hydrogen-peroxide oxidoreductase, Horseradish peroxidase\u003c\/p\u003e\n\u003cp\u003e\u003cstrong\u003eGeneral description\u003c\/strong\u003e\u003cbr\u003eHorseradish peroxidase is isolated from horseradish roots (Amoracia rusticana) and belongs to the ferroprotoporphyrin group of peroxidases. HRP is a single chain polypeptide containing four disulfide bridges. It is a glycoprotein containing 18% carbohydrate. The carbohydrate composition consists of galactose, arabinose, xylose, fucose, mannose, mannosamine, and galactosamine depending upon the specific isozyme. Its molecular weight (~44 kDa) includes the polypeptide chain (33,890 Daltons), hemin plus Ca2+ (~700 Daltons), and carbohydrate (~9,400 Daltons). At least seven isozymes of HRP exist. The isoelectric point for horseradish peroxidase isozymes ranges from 3.0 - 9.0.\u003c\/p\u003e\n\u003cp\u003e\u003cstrong\u003eApplication\u003c\/strong\u003e\u003cbr\u003eHorseradish peroxidase (HRP) is isolated from horseradish roots (Amoracia rusticana). It is used in biochemistry applications such as western blots, ELISA and Immunohistochemistry. Horseradish peroxidase is used to amplify a weak signal and increase detectability of a target molecule, such as a protein. Product P6782 is type VI-A and it is essentially a salt-free, lyophilized powder. It is used to quantify cholesterol and cholesterol esters[1] and to study in vitro lipid deposition on hydrogel and silicone hydrogel contact lenses[2].\u003c\/p\u003e\n\u003cp\u003eThe enzyme from Sigma has been used in the development of rapid and sensitive galactose oxidase-peroxidase biosensor for galactose detection with prolonged stability.[3] It has been used as a component of a media (MRS agar) plate containing 3,3′,5,5′-tetramethylbenzidine (TMB) for the growth of Lactobacillus sp. TMB acts as a chromogenic substrate of peroxidase. Peroxidase generates O2 from H2O2 produced by the lactobacilli, and the TMB stains the colonies blue in the presence of O2. Thus, after 48 hours of incubation under 5% CO2 in air, the colonies that produce H2O2 on MRS agar appear dark blue. H2O2 nonproducers are colorless.[4] It has been used to study the stabilization effect of polyvinyl alcohol on horseradish peroxidase.[5] It is also used for the determination of glucose[6] and peroxides[7] in solution.\u003c\/p\u003e\n\u003cp\u003e\u003cstrong\u003eBiochem\/physiol Actions\u003c\/strong\u003e\u003cbr\u003eHRP readily combines with hydrogen peroxide (H2O2) and the resultant [HRP-H2O2] complex can oxidize a wide variety of hydrogen donors. The optimal pH is 6.0-6.5 and the enzyme is most stable in the pH range of 5.0-9.0. HRP can be conjugated to antibodies by several different methods that include the use of glutaraldehyde, periodate oxidation, disulfide bonds, and also via amino and thiol directed cross-linkers. It is smaller and more stable than the enzyme labels, β-galactosidase and alkaline phosphatase. Hence, it is the most desired label. Also, its glycosylation leads to lower non-specific binding.[8] Sodium azide, cyanide, L-cystine, dichromate, ethylenethiourea, hydroxylamine, sulfide, vanadate, p-aminobenzoic acid, as well as Cd2+, Co2+, Cu2+, Fe3+, Mn2+, Ni2+, and Pb2+ ions are found to inhibit the enzyme activity.[9]\u003c\/p\u003e\n\u003cp\u003eWhen incubated with a substrate, horseradish peroxidase produces a coloured, fluorimetric, or luminescent derivative of the labeled molecule, allowing quantification. Horseradish peroxidase has been shown to slightly reduce the level of inhibition in a cydAB mutant.\u003c\/p\u003e\n\u003cp\u003e\u003cstrong\u003ePackaging\u003c\/strong\u003e\u003cbr\u003ePackaged in mg solid\u003c\/p\u003e\n\u003cp\u003e\u003cstrong\u003ePreparation Note\u003c\/strong\u003e\u003cbr\u003eSolutions of this product at 1 mg\/mL in 0.1 M phosphate buffer (pH 6.0) remain active for at least two weeks at room temperature. The solution retains activity after 5 freeze-thaw cycles.\u003c\/p\u003e\n\u003cp\u003e\u003cstrong\u003eAnalysis Note\u003c\/strong\u003e\u003cbr\u003eThe RZ (Reinheitszahl) is the absorbance ratio A403\/A275 determined at 0.5-1.0 mg\/ml in deionized water. It is a measure of hemin content, not enzymatic activity. Even preparations with high RZ may have low enzymatic activity.\u003cbr\u003eThis product is assayed using ABTS for easy comparison to other suppliers′ unit: approx. 1,000 units per mg solid\u003c\/p\u003e\n\u003cp\u003e\u003cstrong\u003eOther Notes\u003c\/strong\u003e\u003cbr\u003eOne ABTS unit will oxidize 1 μmole of ABTS per minute at 25 °C at pH 5.0\u003cbr\u003eOne pyrogallol unit will form 1.0 mg purpurogallin from pyrogallol in 20 sec at pH 6.0 at 20 °C.\u003cbr\u003eSimilar to P8375\u003c\/p\u003e","brand":"Millipore Sigma","offers":[{"title":"Default Title","offer_id":43042844999739,"sku":"P8250-200KU","price":1462.5,"currency_code":"USD","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0606\/5641\/8875\/files\/P8250-200KU_74a96b99-5cc2-4209-97be-b07d90b107e4.png?v=1764188024"},{"product_id":"millipore-glucose-oxidase-peroxidase-reagent-assay-kits","title":"Glucose oxidase\/peroxidase reagent for Assay Kits","description":"\u003cp\u003e\u003cstrong\u003eGlucose oxidase\/peroxidase reagent\u003c\/strong\u003e\u003cbr\u003efor use with enzymatic assay kits GAGO20, STA20\u003c\/p\u003e\n\u003cp\u003eSynonym(s): GOD-POD Reagent\u003c\/p\u003e\n\u003cp\u003e\u003cstrong\u003eDescription\u003c\/strong\u003e\u003c\/p\u003e\n\u003cp\u003eGlucose Oxidase\/Peroxidase Reagent (GOD–POD) is a ready-to-use enzymatic reagent blend designed for the quantitative determination of glucose in biological, food, beverage, fermentation, and research samples. This reagent is used in combination with O-dianisidine (or comparable chromogenic substrates) within enzymatic colorimetric glucose assays.\u003cbr\u003eThe reagent contains glucose oxidase (GOD) and horseradish peroxidase (POD), enabling a two-step coupled reaction. Glucose oxidase converts β-D-glucose to D-glucono-δ-lactone and hydrogen peroxide; peroxidase then catalyzes the oxidation of a chromogenic substrate, generating a measurable colored product suitable for photometric detection.\u003cbr\u003eThis reagent is fully compatible with Sigma’s GAGO20 and STA20 assay kits and is widely used for determining glucose levels in plasma, serum, urine, and general analytical applications.\u003c\/p\u003e\n\u003cp\u003e\u003cstrong\u003eApplication\u003c\/strong\u003e\u003cbr\u003eGlucose oxidase\/peroxidase reagent along with O-Dianisidine was used for the determination of blood and urinary glucose, especially the presence of fructose for both research and clinical purpose.[1] It may be used for determining glucose in plasma or serum.[2] It may also be used in the estimation of blood glucose as a function of the oxidative coupling system or of the oxygen affinity of the oxygen acceptor chromogen.\u003c\/p\u003e","brand":"Millipore Sigma","offers":[{"title":"Default Title","offer_id":43042845130811,"sku":"G3660-1CAP","price":56.5,"currency_code":"USD","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0606\/5641\/8875\/files\/G3660-1CAP_2176ef8b-8c6b-4ff8-98fb-1fad3079b5d1.png?v=1764188025"},{"product_id":"millipore-o-dianisidine-dihydrochloride-5mg","title":"o-Dianisidine dihydrochloride 5MG","description":"\u003cp\u003e\u003cstrong\u003eo-Dianisidine dihydrochloride\u003c\/strong\u003e\u003cbr\u003evial of 5 mg\u003c\/p\u003e\n\u003cp\u003eSynonym(s): o-Dianisidine reagent\u003c\/p\u003e\n\u003cp\u003e\u003cstrong\u003eDescription\u003c\/strong\u003e\u003c\/p\u003e\n\u003cp\u003eo-Dianisidine Dihydrochloride is a chromogenic substrate used in colorimetric glucose assays based on the glucose oxidase–peroxidase (GOD–POD) reaction. In the presence of glucose oxidase and horseradish peroxidase, o-dianisidine is oxidized by hydrogen peroxide to produce a measurable colored product, enabling sensitive detection of glucose in food, beverages, fermentation samples, biological fluids, and general analytical workflows.\u003cbr\u003e\u003c\/p\u003e\n\u003cp\u003eThis material is provided as a 5 mg solid reagent suitable for photometric detection at 430–540 nm (depending on the oxidized chromophore). It is widely used in assay kits and laboratory protocols requiring rapid, reliable, and high-contrast color development.\u003c\/p\u003e\n\u003cp\u003e\u003cstrong\u003eApplication\u003c\/strong\u003e\u003cbr\u003eIndicator substrate for the quantitative determination of glucose in food and other materials utilizing the glucose oxidase-peroxidase-o-dianisidine enzymatic assay.\u003c\/p\u003e","brand":"Millipore Sigma","offers":[{"title":"Default Title","offer_id":43042845261883,"sku":"D2679-1VL","price":39.69,"currency_code":"USD","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0606\/5641\/8875\/files\/D2679-1VL_e01d7944-8b1c-4e0b-b932-a141ca0c1186.png?v=1764188025"},{"product_id":"millipore-glucose-oxidase-aspergillus-niger-xs-10ku","title":"Glucose Oxidase from Aspergillus niger Type X-S - 10,000 units","description":"\u003cp\u003e\u003cstrong\u003eGlucose Oxidase from Aspergillus niger\u003c\/strong\u003eType X-S, lyophilized powder, 100,000-250,000 units\/g solid (without added oxygen)\u003cbr\u003e\u003c\/p\u003e\n\u003cp\u003eSynonym(s): β-D-Glucose:oxygen 1-oxidoreductase, G.Od., GOx\u003c\/p\u003e\n\u003cp\u003e\u003cstrong\u003eGeneral description\u003c\/strong\u003e\u003c\/p\u003e\n\u003cp\u003eGlucose Oxidase (Type X-S) from Aspergillus niger is a high-purity, lyophilized enzyme preparation delivering 100,000–250,000 units\/g solid (without added oxygen). This FAD-dependent oxidase is a homodimer (~160 kDa) widely used in glucose assays, biosensors, fuel-cell development, food analysis, oxidative stress models, pharmaceutical workflows, and diagnostic assay manufacturing.\u003cbr\u003e\u003c\/p\u003e\n\u003cp\u003eThe enzyme selectively oxidizes β-D-glucose to D-glucono-β-lactone and hydrogen peroxide. With a pH optimum of 5.5 and a broad operating range (pH 4–7), this preparation performs effectively across analytical, industrial, and electrochemical environments. The material is shipped on wet ice and requires −20 °C storage.\u003cbr\u003eThis Type X-S material is designated a Greener Alternative Product, supporting waste prevention and energy efficiency principles when used in fuel-cell and biosensor research.\u003c\/p\u003e","brand":"Millipore Sigma","offers":[{"title":"Default Title","offer_id":43042874753083,"sku":"G7141-10KU","price":85.25,"currency_code":"USD","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0606\/5641\/8875\/files\/G7141_d558915a-acb6-4208-bbeb-949227463cd8.png?v=1764188004"},{"product_id":"millipore-glucose-oxidase-aspergillus-niger-xs-50ku","title":"Glucose Oxidase from Aspergillus niger Type X-S - 50,000 units","description":"\u003cp\u003e\u003cstrong\u003eGlucose Oxidase from Aspergillus niger\u003c\/strong\u003e\u003cbr\u003eType X-S, lyophilized powder, 100,000-250,000 units\/g solid (without added oxygen)\u003cbr\u003e\u003c\/p\u003e\n\u003cp\u003eSynonym(s): β-D-Glucose:oxygen 1-oxidoreductase, G.Od., GOx\u003c\/p\u003e\n\u003cp\u003e\u003cstrong\u003eGeneral description\u003c\/strong\u003e\u003c\/p\u003e\n\u003cp\u003eGlucose Oxidase (Type X-S) from Aspergillus niger is a high-purity, lyophilized enzyme preparation delivering 100,000–250,000 units\/g solid (without added oxygen). This FAD-dependent oxidase is a homodimer (~160 kDa) widely used in glucose assays, biosensors, fuel-cell development, food analysis, oxidative stress models, pharmaceutical workflows, and diagnostic assay manufacturing.\u003cbr\u003e\u003c\/p\u003e\n\u003cp\u003eThe enzyme selectively oxidizes β-D-glucose to D-glucono-β-lactone and hydrogen peroxide. With a pH optimum of 5.5 and a broad operating range (pH 4–7), this preparation performs effectively across analytical, industrial, and electrochemical environments. The material is shipped on wet ice and requires −20 °C storage.\u003cbr\u003eThis Type X-S material is designated a Greener Alternative Product, supporting waste prevention and energy efficiency principles when used in fuel-cell and biosensor research.\u003c\/p\u003e","brand":"Millipore Sigma","offers":[{"title":"Default Title","offer_id":43042874818619,"sku":"G7141-50KU","price":176.25,"currency_code":"USD","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0606\/5641\/8875\/files\/G7141_5826b5fa-cc8a-46b5-bfab-527bbf3b44dd.png?v=1764188006"},{"product_id":"millipore-glucose-oxidase-aspergillus-niger-xs-250ku","title":"Glucose Oxidase from Aspergillus niger Type X-S - 250,000 units","description":"\u003cp\u003e\u003cstrong\u003eGlucose Oxidase from Aspergillus niger\u003c\/strong\u003e\u003cbr\u003eType X-S, lyophilized powder, 100,000-250,000 units\/g solid (without added oxygen)\u003cbr\u003e\u003c\/p\u003e\n\u003cp\u003eSynonym(s): β-D-Glucose:oxygen 1-oxidoreductase, G.Od., GOx\u003c\/p\u003e\n\u003cp\u003e\u003cstrong\u003eGeneral description\u003c\/strong\u003e\u003c\/p\u003e\n\u003cp\u003eGlucose Oxidase (Type X-S) from Aspergillus niger is a high-purity, lyophilized enzyme preparation delivering 100,000–250,000 units\/g solid (without added oxygen). This FAD-dependent oxidase is a homodimer (~160 kDa) widely used in glucose assays, biosensors, fuel-cell development, food analysis, oxidative stress models, pharmaceutical workflows, and diagnostic assay manufacturing.\u003cbr\u003e\u003c\/p\u003e\n\u003cp\u003eThe enzyme selectively oxidizes β-D-glucose to D-glucono-β-lactone and hydrogen peroxide. With a pH optimum of 5.5 and a broad operating range (pH 4–7), this preparation performs effectively across analytical, industrial, and electrochemical environments. The material is shipped on wet ice and requires −20 °C storage.\u003cbr\u003eThis Type X-S material is designated a Greener Alternative Product, supporting waste prevention and energy efficiency principles when used in fuel-cell and biosensor research.\u003c\/p\u003e","brand":"Millipore Sigma","offers":[{"title":"Default Title","offer_id":43042875015227,"sku":"G7141-250KU","price":662.5,"currency_code":"USD","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0606\/5641\/8875\/files\/G7141_e94832fe-8f71-41df-853c-516b62559832.png?v=1764188007"},{"product_id":"millipore-glucose-oxidase-aspergillus-niger-xs-1mu","title":"Glucose Oxidase from Aspergillus niger Type X-S - 1,000,000 units","description":"\u003cp\u003e\u003cstrong\u003eGlucose Oxidase from Aspergillus niger\u003c\/strong\u003e\u003cbr\u003e\u003c\/p\u003e\n\u003cp\u003eType X-S, lyophilized powder, 100,000-250,000 units\/g solid (without added oxygen)\u003cbr\u003e\u003c\/p\u003e\n\u003cp\u003eSynonym(s): β-D-Glucose:oxygen 1-oxidoreductase, G.Od., GOx\u003c\/p\u003e\n\u003cp\u003e\u003cstrong\u003eGeneral description\u003c\/strong\u003e\u003c\/p\u003e\n\u003cp\u003eGlucose Oxidase (Type X-S) from Aspergillus niger is a high-purity, lyophilized enzyme preparation delivering 100,000–250,000 units\/g solid (without added oxygen). This FAD-dependent oxidase is a homodimer (~160 kDa) widely used in glucose assays, biosensors, fuel-cell development, food analysis, oxidative stress models, pharmaceutical workflows, and diagnostic assay manufacturing.\u003cbr\u003e\u003c\/p\u003e\n\u003cp\u003eThe enzyme selectively oxidizes β-D-glucose to D-glucono-β-lactone and hydrogen peroxide. With a pH optimum of 5.5 and a broad operating range (pH 4–7), this preparation performs effectively across analytical, industrial, and electrochemical environments. The material is shipped on wet ice and requires −20 °C storage.\u003cbr\u003eThis Type X-S material is designated a Greener Alternative Product, supporting waste prevention and energy efficiency principles when used in fuel-cell and biosensor research.\u003c\/p\u003e","brand":"Millipore Sigma","offers":[{"title":"Default Title","offer_id":43042875211835,"sku":"G7141-1MU","price":1900.0,"currency_code":"USD","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0606\/5641\/8875\/files\/G7141_8fdf13f6-3e46-45d9-bc97-98bfc6c7ce69.png?v=1764188009"},{"product_id":"millipore-glucose-oxidase-aspergillus-niger-xs-2-5mu","title":"Glucose Oxidase from Aspergillus niger Type X-S - 2,500,000 units","description":"\u003cp\u003e\u003cstrong\u003eGlucose Oxidase from Aspergillus niger\u003c\/strong\u003e\u003cbr\u003eType X-S, lyophilized powder, 100,000-250,000 units\/g solid (without added oxygen)\u003cbr\u003e\u003c\/p\u003e\n\u003cp\u003eSynonym(s): β-D-Glucose:oxygen 1-oxidoreductase, G.Od., GOx\u003c\/p\u003e\n\u003cp\u003e\u003cstrong\u003eGeneral description\u003c\/strong\u003e\u003c\/p\u003e\n\u003cp\u003eGlucose Oxidase (Type X-S) from Aspergillus niger is a high-purity, lyophilized enzyme preparation delivering 100,000–250,000 units\/g solid (without added oxygen). This FAD-dependent oxidase is a homodimer (~160 kDa) widely used in glucose assays, biosensors, fuel-cell development, food analysis, oxidative stress models, pharmaceutical workflows, and diagnostic assay manufacturing.\u003cbr\u003e\u003c\/p\u003e\n\u003cp\u003eThe enzyme selectively oxidizes β-D-glucose to D-glucono-β-lactone and hydrogen peroxide. With a pH optimum of 5.5 and a broad operating range (pH 4–7), this preparation performs effectively across analytical, industrial, and electrochemical environments. The material is shipped on wet ice and requires −20 °C storage.\u003cbr\u003eThis Type X-S material is designated a Greener Alternative Product, supporting waste prevention and energy efficiency principles when used in fuel-cell and biosensor research.\u003c\/p\u003e","brand":"Millipore Sigma","offers":[{"title":"Default Title","offer_id":43042875244603,"sku":"G7141-2.5MU","price":4125.0,"currency_code":"USD","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0606\/5641\/8875\/files\/G7141_93d59237-b8f5-4944-8e03-d48b501e71ce.png?v=1764188010"},{"product_id":"millipore-trolox-97-5g","title":"(±)-6-Hydroxy-2,5,7,8-tetramethylchromane-2-carboxylic Acid, 97% - 5g","description":"\u003cp\u003e(±)-6-Hydroxy-2,5,7,8-tetramethylchromane-2-carboxylic acid, commonly known as Trolox, is a water-soluble vitamin E analog supplied at 97% purity. It is widely used as a reference antioxidant compound in biochemical and analytical research.\u003c\/p\u003e\n\n\u003cp\u003eTrolox exhibits strong radical scavenging and antioxidant activity and is frequently used in Trolox Equivalent Antioxidant Capacity (TEAC) assays to quantify total antioxidant capacity in biological samples, food extracts, and plant materials. Due to its defined antioxidant potential, it serves as a standard for comparative oxidative stress and free radical studies.\u003c\/p\u003e","brand":"Millipore Sigma","offers":[{"title":"Default Title","offer_id":43255754948667,"sku":"238813-5G","price":252.0,"currency_code":"USD","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0606\/5641\/8875\/files\/6-Hydroxy-2_5_7_8-tetramethylchromane-2-carboxylic_acid.png?v=1772036878"},{"product_id":"millipore-trolox-97-1g","title":"(±)-6-Hydroxy-2,5,7,8-tetramethylchromane-2-carboxylic Acid, 97% - 1g","description":"\u003cp\u003e(±)-6-Hydroxy-2,5,7,8-tetramethylchromane-2-carboxylic acid, commonly known as Trolox, is a water-soluble vitamin E analog supplied at 97% purity. It is widely used as a reference antioxidant compound in biochemical and analytical research.\u003c\/p\u003e\n\n\u003cp\u003eTrolox exhibits strong radical scavenging and antioxidant activity and is frequently used in Trolox Equivalent Antioxidant Capacity (TEAC) assays to quantify total antioxidant capacity in biological samples, food extracts, and plant materials. Due to its defined antioxidant potential, it serves as a standard for comparative oxidative stress and free radical studies.\u003c\/p\u003e","brand":"Millipore Sigma","offers":[{"title":"Default Title","offer_id":43255754981435,"sku":"238813-1G","price":101.0,"currency_code":"USD","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0606\/5641\/8875\/files\/6-Hydroxy-2_5_7_8-tetramethylchromane-2-carboxylic_acid.png?v=1772036878"},{"product_id":"millipore-potassium-hydroxide-reagent-90-10kg","title":"Potassium Hydroxide, Reagent Grade, 90%, Flakes - 10KG","description":"\u003cp\u003ePotassium hydroxide (KOH), reagent grade, 90% assay, is supplied in flake form for laboratory and industrial applications. Also known as caustic potash, KOH is a strong, hygroscopic base with high water solubility.\u003c\/p\u003e\n\n\u003cp\u003eIt is widely used in analytical chemistry, buffer preparation, saponification reactions, base-catalyzed syntheses, and environmental testing methods. This grade is suitable for EPA 1613 and SM 5210 applications. Potassium hydroxide is also utilized in organic synthesis, silicon etching, CO₂ absorption, and general laboratory neutralization procedures.\u003c\/p\u003e","brand":"Millipore Sigma","offers":[{"title":"Default Title","offer_id":43255756849211,"sku":"484016-10KG","price":298.0,"currency_code":"USD","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0606\/5641\/8875\/files\/Potassium_hydroxide.png?v=1772473878"},{"product_id":"millipore-potassium-hydroxide-reagent-90-1kg","title":"Potassium Hydroxide, Reagent Grade, 90%, Flakes - 1KG","description":"\u003cp\u003ePotassium hydroxide (KOH), reagent grade, 90% assay, is supplied in flake form for laboratory and industrial applications. Also known as caustic potash, KOH is a strong, hygroscopic base with high water solubility.\u003c\/p\u003e\n\n\u003cp\u003eIt is widely used in analytical chemistry, buffer preparation, saponification reactions, base-catalyzed syntheses, and environmental testing methods. This grade is suitable for EPA 1613 and SM 5210 applications. Potassium hydroxide is also utilized in organic synthesis, silicon etching, CO₂ absorption, and general laboratory neutralization procedures.\u003c\/p\u003e","brand":"Millipore Sigma","offers":[{"title":"Default Title","offer_id":43255756881979,"sku":"484016-1KG","price":68.0,"currency_code":"USD","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0606\/5641\/8875\/files\/Potassium_hydroxide.png?v=1772473878"},{"product_id":"millipore-cellulose-fibers-m-1kg","title":"Cellulose Fibers (Medium) - 1KG","description":"\u003cp\u003eCellulose is a naturally occurring β-1,4-linked polysaccharide composed of linear glucose units and is a primary structural component of plant cell walls. Supplied here as medium particle size fibers derived from softwood tree pulp, this cellulose material is suitable for research, chromatography, biomass analysis, and carbohydrate-related applications.\u003c\/p\u003e\n\n\u003cp\u003eThis product is commonly used in metabolic pathway studies, biofuel and biorefinery research, FTIR analysis, and as a chromatography support material. Its fibrous structure and defined particle size make it appropriate for laboratory-scale analytical and preparative work.\u003c\/p\u003e","brand":"Millipore Sigma","offers":[{"title":"Default Title","offer_id":43255758028859,"sku":"C6288-1KG","price":362.0,"currency_code":"USD","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0606\/5641\/8875\/files\/Cellulose.png?v=1772581287"},{"product_id":"millipore-cellulose-fibers-m-250g","title":"Cellulose Fibers (Medium) - 250g","description":"\u003cp\u003eCellulose is a naturally occurring β-1,4-linked polysaccharide composed of linear glucose units and is a primary structural component of plant cell walls. Supplied here as medium particle size fibers derived from softwood tree pulp, this cellulose material is suitable for research, chromatography, biomass analysis, and carbohydrate-related applications.\u003c\/p\u003e\n\n\u003cp\u003eThis product is commonly used in metabolic pathway studies, biofuel and biorefinery research, FTIR analysis, and as a chromatography support material. Its fibrous structure and defined particle size make it appropriate for laboratory-scale analytical and preparative work.\u003c\/p\u003e","brand":"Millipore Sigma","offers":[{"title":"Default Title","offer_id":43255758061627,"sku":"C6288-250G","price":119.0,"currency_code":"USD","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0606\/5641\/8875\/files\/Cellulose.png?v=1772581287"},{"product_id":"millipore-cellulose-fibers-m-100g","title":"Cellulose Fibers (Medium) - 100g","description":"\u003cp\u003eCellulose is a naturally occurring β-1,4-linked polysaccharide composed of linear glucose units and is a primary structural component of plant cell walls. Supplied here as medium particle size fibers derived from softwood tree pulp, this cellulose material is suitable for research, chromatography, biomass analysis, and carbohydrate-related applications.\u003c\/p\u003e\n\n\u003cp\u003eThis product is commonly used in metabolic pathway studies, biofuel and biorefinery research, FTIR analysis, and as a chromatography support material. Its fibrous structure and defined particle size make it appropriate for laboratory-scale analytical and preparative work.\u003c\/p\u003e","brand":"Millipore Sigma","offers":[{"title":"Default Title","offer_id":43255758094395,"sku":"C6288-100G","price":65.0,"currency_code":"USD","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0606\/5641\/8875\/files\/Cellulose.png?v=1772581287"},{"product_id":"millipore-choline-chloride-trimethyl-d9-98-1g","title":"Choline Chloride-(Trimethyl-d9), 98 atom % D - 1g","description":"\u003cp\u003eCholine Chloride-(trimethyl-d9) is a deuterium-labeled isotopic analogue of choline chloride containing 98 atom % deuterium. This stable isotope compound is commonly used in mass spectrometry applications as an internal standard and tracer for quantitative analysis.\u003c\/p\u003e\n\n\u003cp\u003eThe compound exhibits a mass shift of M+9 and is suitable for metabolic, lipidomics, and betaine pathway studies. It is also used in the investigation of deep eutectic solvent structure and hydration behavior.\u003c\/p\u003e","brand":"Millipore Sigma","offers":[{"title":"Default Title","offer_id":43255758323771,"sku":"492051-1G","price":371.0,"currency_code":"USD","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0606\/5641\/8875\/files\/Choline_chloride-_trimethyl-d9.png?v=1772585807"},{"product_id":"millipore-polymyxin-b-sulfatemeets-50mu","title":"Polymyxin B sulfate - meets USP testing specifications - 50MU","description":"\u003cp\u003ePolymyxin B sulfate is a cyclic polypeptide antibiotic derived from Bacillus polymyxa, supplied as a USP\/NF grade material meeting United States Pharmacopeia testing specifications. It is commonly used in pharmaceutical and microbiological applications, particularly for antimicrobial studies and analytical workflows involving Gram-negative bacteria.\u003c\/p\u003e\n\n\u003cp\u003eThis compound exhibits strong bactericidal activity by binding to the lipid A portion of bacterial lipopolysaccharides, disrupting membrane integrity and increasing permeability. Due to this mechanism, polymyxin B sulfate is widely used in studies of membrane biology, endotoxin removal, and antimicrobial resistance.\u003c\/p\u003e\n\n\u003cp\u003eIn laboratory settings, polymyxin B sulfate is utilized in pharmaceutical analysis, microbiological assays, and research involving bacterial susceptibility and permeability studies. It is also applied in sample preparation workflows where selective inhibition of Gram-negative organisms is required.\u003c\/p\u003e\n\n\u003cp\u003eThis material is provided as a powder and is suitable for use in regulated laboratory environments requiring USP-compliant substances.\u003c\/p\u003e","brand":"Millipore Sigma","offers":[{"title":"Default Title","offer_id":43389805363259,"sku":"P0972-50MU","price":1820.0,"currency_code":"USD","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0606\/5641\/8875\/files\/Polymyxin_B_sulfate.png?v=1774650318"},{"product_id":"millipore-polymyxin-b-sulfatemeets-10mu","title":"Polymyxin B sulfate - meets USP testing specifications - 10MU","description":"\u003cp\u003ePolymyxin B sulfate is a cyclic polypeptide antibiotic derived from Bacillus polymyxa, supplied as a USP\/NF grade material meeting United States Pharmacopeia testing specifications. It is commonly used in pharmaceutical and microbiological applications, particularly for antimicrobial studies and analytical workflows involving Gram-negative bacteria.\u003c\/p\u003e\n\n\u003cp\u003eThis compound exhibits strong bactericidal activity by binding to the lipid A portion of bacterial lipopolysaccharides, disrupting membrane integrity and increasing permeability. Due to this mechanism, polymyxin B sulfate is widely used in studies of membrane biology, endotoxin removal, and antimicrobial resistance.\u003c\/p\u003e\n\n\u003cp\u003eIn laboratory settings, polymyxin B sulfate is utilized in pharmaceutical analysis, microbiological assays, and research involving bacterial susceptibility and permeability studies. It is also applied in sample preparation workflows where selective inhibition of Gram-negative organisms is required.\u003c\/p\u003e\n\n\u003cp\u003eThis material is provided as a powder and is suitable for use in regulated laboratory environments requiring USP-compliant substances.\u003c\/p\u003e","brand":"Millipore Sigma","offers":[{"title":"Default Title","offer_id":43389805396027,"sku":"P0972-10MU","price":514.0,"currency_code":"USD","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0606\/5641\/8875\/files\/Polymyxin_B_sulfate.png?v=1774650318"},{"product_id":"millipore-polymyxin-b-sulfatemeets-1mu","title":"Polymyxin B sulfate - meets USP testing specifications - 1MU","description":"\u003cp\u003ePolymyxin B sulfate is a cyclic polypeptide antibiotic derived from Bacillus polymyxa, supplied as a USP\/NF grade material meeting United States Pharmacopeia testing specifications. It is commonly used in pharmaceutical and microbiological applications, particularly for antimicrobial studies and analytical workflows involving Gram-negative bacteria.\u003c\/p\u003e\n\n\u003cp\u003eThis compound exhibits strong bactericidal activity by binding to the lipid A portion of bacterial lipopolysaccharides, disrupting membrane integrity and increasing permeability. Due to this mechanism, polymyxin B sulfate is widely used in studies of membrane biology, endotoxin removal, and antimicrobial resistance.\u003c\/p\u003e\n\n\u003cp\u003eIn laboratory settings, polymyxin B sulfate is utilized in pharmaceutical analysis, microbiological assays, and research involving bacterial susceptibility and permeability studies. It is also applied in sample preparation workflows where selective inhibition of Gram-negative organisms is required.\u003c\/p\u003e\n\n\u003cp\u003eThis material is provided as a powder and is suitable for use in regulated laboratory environments requiring USP-compliant substances.\u003c\/p\u003e","brand":"Millipore Sigma","offers":[{"title":"Default Title","offer_id":43389805428795,"sku":"P0972-1MU","price":104.0,"currency_code":"USD","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0606\/5641\/8875\/files\/Polymyxin_B_sulfate.png?v=1774650318"},{"product_id":"millipore-bovine-collagen-type-i-powder-25g","title":"Bovine Collagen Type I, Powder - 25 G","description":"\u003cp\u003eBovine Collagen Type I is a structural protein isolated from bovine Achilles tendon and supplied as a powder suitable for biochemical and analytical applications. Type I collagen is the most abundant collagen in mammalian connective tissue and plays a key role in extracellular matrix structure and function.\u003c\/p\u003e\n\n\u003cp\u003eThis material is commonly used as a substrate for collagenase activity assays and is suitable for ELISA-based techniques and other biochemical assays. It is widely applied in studies involving tissue structure, enzyme activity, protein interactions, and extracellular matrix research.\u003c\/p\u003e\n\n\u003cp\u003eDue to its fibrous and insoluble nature, collagen Type I is typically prepared as a suspension for enzymatic or analytical applications. It is used in life science research, pharmaceutical development, and biomaterials studies where controlled collagen substrates are required.\u003c\/p\u003e","brand":"Millipore Sigma","offers":[{"title":"Default Title","offer_id":43389805723707,"sku":"C9879-25G","price":996.0,"currency_code":"USD","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0606\/5641\/8875\/files\/Bovine_Collagen_Type_I.png?v=1774656134"},{"product_id":"millipore-bovine-collagen-type-i-powder-10g","title":"Bovine Collagen Type I, Powder - 10 G","description":"\u003cp\u003eBovine Collagen Type I is a structural protein isolated from bovine Achilles tendon and supplied as a powder suitable for biochemical and analytical applications. Type I collagen is the most abundant collagen in mammalian connective tissue and plays a key role in extracellular matrix structure and function.\u003c\/p\u003e\n\n\u003cp\u003eThis material is commonly used as a substrate for collagenase activity assays and is suitable for ELISA-based techniques and other biochemical assays. It is widely applied in studies involving tissue structure, enzyme activity, protein interactions, and extracellular matrix research.\u003c\/p\u003e\n\n\u003cp\u003eDue to its fibrous and insoluble nature, collagen Type I is typically prepared as a suspension for enzymatic or analytical applications. It is used in life science research, pharmaceutical development, and biomaterials studies where controlled collagen substrates are required.\u003c\/p\u003e","brand":"Millipore Sigma","offers":[{"title":"Default Title","offer_id":43389805756475,"sku":"C9879-10G","price":516.0,"currency_code":"USD","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0606\/5641\/8875\/files\/Bovine_Collagen_Type_I.png?v=1774656134"},{"product_id":"millipore-bovine-collagen-type-i-powder-5g","title":"Bovine Collagen Type I, Powder - 5 G","description":"\u003cp\u003eBovine Collagen Type I is a structural protein isolated from bovine Achilles tendon and supplied as a powder suitable for biochemical and analytical applications. Type I collagen is the most abundant collagen in mammalian connective tissue and plays a key role in extracellular matrix structure and function.\u003c\/p\u003e\n\n\u003cp\u003eThis material is commonly used as a substrate for collagenase activity assays and is suitable for ELISA-based techniques and other biochemical assays. It is widely applied in studies involving tissue structure, enzyme activity, protein interactions, and extracellular matrix research.\u003c\/p\u003e\n\n\u003cp\u003eDue to its fibrous and insoluble nature, collagen Type I is typically prepared as a suspension for enzymatic or analytical applications. It is used in life science research, pharmaceutical development, and biomaterials studies where controlled collagen substrates are required.\u003c\/p\u003e","brand":"Millipore Sigma","offers":[{"title":"Default Title","offer_id":43389805789243,"sku":"C9879-5G","price":394.0,"currency_code":"USD","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0606\/5641\/8875\/files\/Bovine_Collagen_Type_I.png?v=1774656134"},{"product_id":"millipore-bovine-collagen-type-i-powder-1g","title":"Bovine Collagen Type I, Powder - 1 G","description":"\u003cp\u003eBovine Collagen Type I is a structural protein isolated from bovine Achilles tendon and supplied as a powder suitable for biochemical and analytical applications. Type I collagen is the most abundant collagen in mammalian connective tissue and plays a key role in extracellular matrix structure and function.\u003c\/p\u003e\n\n\u003cp\u003eThis material is commonly used as a substrate for collagenase activity assays and is suitable for ELISA-based techniques and other biochemical assays. It is widely applied in studies involving tissue structure, enzyme activity, protein interactions, and extracellular matrix research.\u003c\/p\u003e\n\n\u003cp\u003eDue to its fibrous and insoluble nature, collagen Type I is typically prepared as a suspension for enzymatic or analytical applications. It is used in life science research, pharmaceutical development, and biomaterials studies where controlled collagen substrates are required.\u003c\/p\u003e","brand":"Millipore Sigma","offers":[{"title":"Default Title","offer_id":43389805822011,"sku":"C9879-1G","price":94.0,"currency_code":"USD","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0606\/5641\/8875\/files\/Bovine_Collagen_Type_I.png?v=1774656134"},{"product_id":"millipore-creatinine-anhydrous-98-1kg","title":"Creatinine, Anhydrous, ≥98% - 1 KG","description":"\u003cp\u003eCreatinine, anhydrous, ≥98%, is a heterocyclic nitrogen-containing compound commonly used in biochemical, clinical, and analytical research applications. It is a metabolic byproduct of creatine phosphate and is widely utilized as a reference compound in studies related to renal function and biochemical pathways.\u003c\/p\u003e\n\n\u003cp\u003eIn laboratory settings, creatinine serves as a building block for nitrogen-containing heterocycles and is used in synthetic chemistry applications, including the preparation of functional materials and catalytic systems. It is also commonly employed in assay development, method validation, and biochemical research.\u003c\/p\u003e\n\n\u003cp\u003eWith high purity and consistent performance, this material is suitable for research, analytical, and general laboratory use.\u003c\/p\u003e","brand":"Millipore Sigma","offers":[{"title":"Default Title","offer_id":43389806215227,"sku":"C4255-1KG","price":1199.0,"currency_code":"USD","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0606\/5641\/8875\/files\/creatine.png?v=1774984051"},{"product_id":"millipore-creatinine-anhydrous-98-100g","title":"Creatinine, Anhydrous, ≥98% - 100 G","description":"\u003cp\u003eCreatinine, anhydrous, ≥98%, is a heterocyclic nitrogen-containing compound commonly used in biochemical, clinical, and analytical research applications. It is a metabolic byproduct of creatine phosphate and is widely utilized as a reference compound in studies related to renal function and biochemical pathways.\u003c\/p\u003e\n\n\u003cp\u003eIn laboratory settings, creatinine serves as a building block for nitrogen-containing heterocycles and is used in synthetic chemistry applications, including the preparation of functional materials and catalytic systems. It is also commonly employed in assay development, method validation, and biochemical research.\u003c\/p\u003e\n\n\u003cp\u003eWith high purity and consistent performance, this material is suitable for research, analytical, and general laboratory use.\u003c\/p\u003e","brand":"Millipore Sigma","offers":[{"title":"Default Title","offer_id":43389806247995,"sku":"C4255-100G","price":226.0,"currency_code":"USD","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0606\/5641\/8875\/files\/creatine.png?v=1774984051"},{"product_id":"millipore-creatinine-anhydrous-98-25g","title":"Creatinine, Anhydrous, ≥98% - 25 G","description":"\u003cp\u003eCreatinine, anhydrous, ≥98%, is a heterocyclic nitrogen-containing compound commonly used in biochemical, clinical, and analytical research applications. It is a metabolic byproduct of creatine phosphate and is widely utilized as a reference compound in studies related to renal function and biochemical pathways.\u003c\/p\u003e\n\n\u003cp\u003eIn laboratory settings, creatinine serves as a building block for nitrogen-containing heterocycles and is used in synthetic chemistry applications, including the preparation of functional materials and catalytic systems. It is also commonly employed in assay development, method validation, and biochemical research.\u003c\/p\u003e\n\n\u003cp\u003eWith high purity and consistent performance, this material is suitable for research, analytical, and general laboratory use.\u003c\/p\u003e","brand":"Millipore Sigma","offers":[{"title":"Default Title","offer_id":43389806280763,"sku":"C4255-25G","price":49.0,"currency_code":"USD","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0606\/5641\/8875\/files\/creatine.png?v=1774984051"},{"product_id":"millipore-creatinine-anhydrous-98-10g","title":"Creatinine, Anhydrous, ≥98% - 10 G","description":"\u003cp\u003eCreatinine, anhydrous, ≥98%, is a heterocyclic nitrogen-containing compound commonly used in biochemical, clinical, and analytical research applications. It is a metabolic byproduct of creatine phosphate and is widely utilized as a reference compound in studies related to renal function and biochemical pathways.\u003c\/p\u003e\n\n\u003cp\u003eIn laboratory settings, creatinine serves as a building block for nitrogen-containing heterocycles and is used in synthetic chemistry applications, including the preparation of functional materials and catalytic systems. It is also commonly employed in assay development, method validation, and biochemical research.\u003c\/p\u003e\n\n\u003cp\u003eWith high purity and consistent performance, this material is suitable for research, analytical, and general laboratory use.\u003c\/p\u003e","brand":"Millipore Sigma","offers":[{"title":"Default Title","offer_id":43389806313531,"sku":"C4255-10G","price":25.0,"currency_code":"USD","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0606\/5641\/8875\/files\/creatine.png?v=1774984051"},{"product_id":"millipore-creatinine-anhydrous-98-10mg","title":"Creatinine, Anhydrous, ≥98% - 10 mg","description":"\u003cp\u003eCreatinine, anhydrous, ≥98%, is a heterocyclic nitrogen-containing compound commonly used in biochemical, clinical, and analytical research applications. It is a metabolic byproduct of creatine phosphate and is widely utilized as a reference compound in studies related to renal function and biochemical pathways.\u003c\/p\u003e\n\n\u003cp\u003eIn laboratory settings, creatinine serves as a building block for nitrogen-containing heterocycles and is used in synthetic chemistry applications, including the preparation of functional materials and catalytic systems. It is also commonly employed in assay development, method validation, and biochemical research.\u003c\/p\u003e\n\n\u003cp\u003eWith high purity and consistent performance, this material is suitable for research, analytical, and general laboratory use.\u003c\/p\u003e","brand":"Millipore Sigma","offers":[{"title":"Default Title","offer_id":43389806346299,"sku":"C4255-10MG","price":22.0,"currency_code":"USD","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0606\/5641\/8875\/files\/creatine.png?v=1774984051"},{"product_id":"millipore-pancreatin-porcine-4xusp-powder-500g","title":"Pancreatin from porcine pancreas, 4× USP, powder - 500 G","description":"\u003cp\u003ePancreatin from porcine pancreas is a multi-enzyme preparation containing protease, amylase, lipase, and other digestive enzymes. Supplied as a powder meeting 4× USP specifications, it is widely used in biochemical, pharmaceutical, and food analysis applications.\u003c\/p\u003e\n\n\u003cp\u003eThis material is commonly utilized for enzymatic digestion studies, in vitro digestibility testing, and sample preparation workflows involving proteins, starches, and lipids. It is also used in microbiological and biochemical research to evaluate enzyme activity and substrate breakdown.\u003c\/p\u003e\n\n\u003cp\u003eWith defined enzymatic activity and consistent performance, pancreatin is suitable for laboratory applications requiring reliable enzymatic hydrolysis across a range of biological and analytical workflows.\u003c\/p\u003e","brand":"Millipore Sigma","offers":[{"title":"Default Title","offer_id":43389806903355,"sku":"P1750-500G","price":365.0,"currency_code":"USD","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0606\/5641\/8875\/files\/PANCREATIN.png?v=1774987278"}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0606\/5641\/8875\/collections\/Enzymes_Biochemicals.png?v=1781040457","url":"https:\/\/gogreenscientific.com\/collections\/enzymes-biochemicals.oembed","provider":"Go Green Scientific","version":"1.0","type":"link"}