345386 Glucose Oxidase, Aspergillus niger, Recombinant

345386
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      Overview

      Replacement Information

      Key Specifications Table

      Pricing & Availability

      Catalog NumberAvailability Packaging Qty/Pack Price Quantity
      345386-10KU
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          Plastic ampoule 10 ku
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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
          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

          Documentation

          SDS

          Title

          Safety Data Sheet (SDS) 

          Certificates of Analysis

          TitleLot Number
          345386

          References

          Reference overview
          Heinz, F. and Beushausen, T.W. 1981. J. Clin. Chem. Clin. Biochem. 19, 977.
          Data Sheet

          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.