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345386 Glucose Oxidase, Aspergillus niger, Recombinant

Glucose Oxidase, Aspergillus niger, Recombinant, CAS 9001-37-0, oxidizes β-D-glucose to D-glucono-ω-lactone and H2O2 and converts D-glucono-ω-lactone to gluconic acid. Useful for assay of glucose.

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345386
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345386-10KU
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      Description
      OverviewRecombinant, Aspergillus niger glucose oxidase. Catalyzes the oxidation of β-D-glucose to D-glucono-ω-lactone and hydrogen peroxide. Also catalyzes the conversion of D-glucono-ω-lactone to gluconic acid. Useful for enzymatic assay of glucose concentration.
      Note: 1 KU = 1000 units.
      Catalogue Number345386
      Brand Family Calbiochem®
      References
      ReferencesHeinz, F. and Beushausen, T.W. 1981. J. Clin. Chem. Clin. Biochem. 19, 977.
      Product Information
      CAS number9001-37-0
      Activity≥250 units/mg solid
      Unit of DefinitionOne unit is defined as the amount of enzyme that will oxidize 1.0 mmol of β-D-glucose per minute at 25°C, pH 7.0.
      EC number1.1.3.4
      FormYellow-brown lyophilized solid
      Quality LevelMQ100
      Applications
      ApplicationGlucose Oxidase, Aspergillus niger, Recombinant, CAS 9001-37-0, oxidizes β-D-glucose to D-glucono-ω-lactone and H2O2 and converts D-glucono-ω-lactone to gluconic acid. Useful for assay of glucose.
      Biological Information
      Physicochemical Information
      ContaminantsAmylase: ≤0.1%; catalase: ≤20 U/mg dry weight; sucrase: ≤0.1%
      Dimensions
      Materials Information
      Toxicological Information
      Safety Information according to GHS
      RTECSRQ8452000
      Safety Information
      Product Usage Statements
      Storage and Shipping Information
      Ship Code Ambient Temperature Only
      Toxicity Standard Handling
      Storage +2°C to +8°C
      Do not freeze Ok to freeze
      Special InstructionsFollowing reconstitution, aliquot and refrigerate (4°C). Stock solutions are stable for up to 3 months at 4°C.
      Packaging Information
      Transport Information
      Supplemental Information
      Specifications
      Global Trade Item Number
      Référence GTIN
      345386-10KU 07790788049300

      Documentation

      Glucose Oxidase, Aspergillus niger, Recombinant FDS

      Titre

      Fiche de données de sécurité des matériaux (FDS) 

      Glucose Oxidase, Aspergillus niger, Recombinant Certificats d'analyse

      TitreNuméro de lot
      345386

      Références bibliographiques

      Aperçu de la référence bibliographique
      Heinz, F. and Beushausen, T.W. 1981. J. Clin. Chem. Clin. Biochem. 19, 977.
      Fiche technique

      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.

      Revision260October-2007 JSW
      DescriptionRecombinant, Aspergillus niger glucose oxidase. Catalyzes the oxidation of β-D-glucose to D-glucono-ω-lactone and hydrogen peroxide. Also catalyzes the conversion of D-glucono-ω-lactone to gluconic acid. Each molecule of enzyme contains 2 molecules of FAD, which are essential for enzyme activity. Optimal pH = 6.5 with > 95% maximal activity at pH 6.0-7.0. Useful for enzymatic assay of glucose. May also be conjugated to antibodies or antigens for use in ELISA procedures.
      FormYellow-brown lyophilized solid
      CAS number9001-37-0
      RTECSRQ8452000
      EC number1.1.3.4
      ContaminantsAmylase: ≤0.1%; catalase: ≤20 U/mg dry weight; sucrase: ≤0.1%
      Activity≥250 units/mg solid
      Unit definitionOne unit is defined as the amount of enzyme that will oxidize 1.0 mmol of β-D-glucose per minute at 25°C, pH 7.0.
      Solubility0.1 M Phosphate buffer, pH 7.0 (5 mg/ml)
      Storage +2°C to +8°C
      Do Not Freeze Ok to freeze
      Special InstructionsFollowing reconstitution, aliquot and refrigerate (4°C). Stock solutions are stable for up to 3 months at 4°C.
      Toxicity Standard Handling
      Merck USA index14, 4460
      ReferencesHeinz, F. and Beushausen, T.W. 1981. J. Clin. Chem. Clin. Biochem. 19, 977.