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682151 Xanthine Oxidase, Buttermilk

Native xanthine oxidase from buttermilk. Complex metalloprotein that catalyzes oxidative hydroxylation of a variety of aromatic heterocycles and simple aldehydes. Catalyzes the oxidation of xanthine to uric acid.

Xanthine Oxidase, Buttermilk MSDS (material safety data sheet) or SDS, CoA and CoQ, dossiers, brochures and other available documents.
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682151
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Overview

Replacement Information

Pricing & Availability

Catalogue Number AvailabilityPackaging Qty/Pack Price Quantity
682151-10U
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      682151-50U
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          Description
          OverviewNative xanthine oxidase from buttermilk. Complex metalloprotein that catalyzes oxidative hydroxylation of a variety of aromatic heterocycles and simple aldehydes. Catalyzes the oxidation of xanthine to uric acid.
          Catalogue Number682151
          Brand Family Calbiochem®
          References
          ReferencesMcWhirter, R.B. and Hille, R. 1991. J. Biol. Chem. 266, 23724.
          Product Information
          CAS number9002-17-9
          Unit of DefinitionOne unit is defined as the amount of enzyme that will convert 1.0 µmol of xanthine to uric acid per min at 25°C, pH 7.5.
          EC number1.1.3.22
          FormLiquid
          FormulationCrystalline suspension in 60% ammonium sulfate.
          HS Code3507 90 39
          PI5.3 - 5.4
          Quality LevelMQ100
          Applications
          Biological Information
          Specific Activity≥0.5 unit/mg protein
          Concentration Label Please refer to vial label for lot-specific concentration
          Physicochemical Information
          Contaminantslactoperoxidase: none
          Dimensions
          Materials Information
          Toxicological Information
          Safety Information according to GHS
          RTECSRQ8455000
          Safety Information
          Product Usage Statements
          Storage and Shipping Information
          Ship Code Blue Ice Only
          Toxicity Standard Handling
          Storage +2°C to +8°C
          Do not freeze Yes
          Canadian export regulations Due to the country and/or U.S. state of origin of the animal material used in this product, this product may not be exported to Canada.
          Packaging Information
          Transport Information
          Supplemental Information
          Specifications
          Global Trade Item Number
          Catalogue Number GTIN
          682151-10U 04055977225310
          682151-50U 04055977225327

          Documentation

          Xanthine Oxidase, Buttermilk SDS

          Title

          Safety Data Sheet (SDS) 

          Xanthine Oxidase, Buttermilk Certificates of Analysis

          TitleLot Number
          682151

          References

          Reference overview
          McWhirter, R.B. and Hille, R. 1991. J. Biol. Chem. 266, 23724.
          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.

          Revision16-September-2008 RFH
          DescriptionNative xanthine oxidase from buttermilk. Complex metalloprotein that catalyzes oxidative hydroxylation of a variety of aromatic heterocycles and simple aldehydes. Has an optimal pH of 4.6 and a pI of 5.3-5.4. Catalyzes the oxidation of xanthine to uric acid.
          FormLiquid
          FormulationCrystalline suspension in 60% ammonium sulfate.
          Concentration Label Please refer to vial label for lot-specific concentration
          CAS number9002-17-9
          RTECSRQ8455000
          EC number1.1.3.22
          Contaminantslactoperoxidase: none
          Specific activity≥0.5 unit/mg protein
          Unit definitionOne unit is defined as the amount of enzyme that will convert 1.0 µmol of xanthine to uric acid per min at 25°C, pH 7.5.
          Storage +2°C to +8°C
          Do Not Freeze Yes
          Toxicity Standard Handling
          ReferencesMcWhirter, R.B. and Hille, R. 1991. J. Biol. Chem. 266, 23724.