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228250 Cholesterol Oxidase, Streptomyces sp.

Cholesterol Oxidase, Streptomyces sp. CAS 9028-76-6, is a native cholesterol oxidase that catalyzes the oxidation of cholesterol to cholesterone and hydrogen peroxide.

Cholesterol Oxidase, Streptomyces sp.: Ficha de datos de seguridad (MSDS o SDS), certificado de análisis y de calidad (CoA y CoQ), expedientes, folletos y otros documentos disponibles.

Sinónimos: Cholesterol:oxygen oxidoreductase

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228250
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228250-500U
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      Description
      OverviewNative cholesterol oxidase from Streptomyces species. Catalyzes oxidation of cholesterol to cholesterone and hydrogen peroxide (isoelectric points: 6.1 and 7.3). Suitable for determination of total cholesterol when coupled with cholinesterase and peroxidase. Has an optimal pH of 6.0-8.0.
      Catalogue Number228250
      Brand Family Calbiochem®
      SynonymsCholesterol:oxygen oxidoreductase
      References
      ReferencesGadda, G., et al. 1997. Eur. J. Biochem. 250, 369.
      Product Information
      CAS number9028-76-6
      Activity≥3 units/mg solid
      Unit of DefinitionOne unit is defined as the amount of enzyme that will oxidize 1.0 µmol of cholesterol per min at 25°C, pH 7.0.
      EC number1.1.3.6
      FormYellow lyophilized solid
      Hygroscopic Hygroscopic
      Quality LevelMQ100
      Applications
      Biological Information
      Specific Activity≥40 units/mg
      Physicochemical Information
      ContaminantsCatalase: ≤1%; glucose oxidase and uricase: ≤0.01%.
      Dimensions
      Materials Information
      Toxicological Information
      Safety Information according to GHS
      Safety Information
      Product Usage Statements
      Storage and Shipping Information
      Ship Code Ambient Temperature Only
      Toxicity Standard Handling
      Storage -20°C
      Protect from Light Protect from light
      Protect from Moisture Protect from moisture
      Hygroscopic Hygroscopic
      Do not freeze Ok to freeze
      Special InstructionsFollowing reconstitution, aliquot and freeze (-20°C). Stock solutions are stable for up to 6 months at -20°C.
      Packaging Information
      Transport Information
      Supplemental Information
      Specifications
      Global Trade Item Number
      Número de referencia GTIN
      228250-500U 04055977218176

      Documentation

      Cholesterol Oxidase, Streptomyces sp. Ficha datos de seguridad (MSDS)

      Título

      Ficha técnica de seguridad del material (MSDS) 

      Cholesterol Oxidase, Streptomyces sp. Certificados de análisis

      CargoNúmero de lote
      228250

      Referencias bibliográficas

      Visión general referencias
      Gadda, G., et al. 1997. Eur. J. Biochem. 250, 369.
      Ficha técnica

      Note that this data sheet is not lot-specific and is representative of the current specifications for this product. Please consult the vial label and the certificate of analysis for information on specific lots. Also note that shipping conditions may differ from storage conditions.

      Revision31-March-2008 JSW
      SynonymsCholesterol:oxygen oxidoreductase
      DescriptionNative cholesterol oxidase from streptomyces species. Catalyzes oxidation of cholesterol to cholesterone and hydrogen peroxide (isoelectric points: 6.1 and 7.3). Suitable for determination of total cholesterol when coupled with cholinesterase and peroxidase. Has an optimal pH of 6.0-8.0.
      FormYellow lyophilized solid
      CAS number9028-76-6
      EC number1.1.3.6
      ContaminantsCatalase: ≤1%; glucose oxidase and uricase: ≤0.01%.
      Specific activity≥40 units/mg
      Activity≥3 units/mg solid
      Unit definitionOne unit is defined as the amount of enzyme that will oxidize 1.0 µmol of cholesterol per min at 25°C, pH 7.0.
      SolubilityH₂O (20 mg/ml)
      Storage Protect from moisture
      Protect from light
      -20°C
      Hygroscopic
      Do Not Freeze Ok to freeze
      Special InstructionsFollowing reconstitution, aliquot and freeze (-20°C). Stock solutions are stable for up to 6 months at -20°C.
      Toxicity Standard Handling
      ReferencesGadda, G., et al. 1997. Eur. J. Biochem. 250, 369.