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574594 Superoxide Dismutase, Bovine Erythrocytes

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574594
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574594-50KU
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      Description
      OverviewNative superoxide dismutase from bovine erythrocytes. Essential component of biological defense against toxic effects of oxygen. Catalyzes the dismutation of superoxide radicals to oxygen and H2O2.
      Note: 1 KU = 1000 units.
      Catalogue Number574594
      Brand Family Calbiochem®
      SynonymsCu/Zn SOD
      References
      ReferencesTilly, J.L. and Tilly, K.I. 1995. Endocrinology 136, 242.
      Sharonov, B.P. and Churilova, I.V. 1992. Biochem. Biophys. Res. Commun. 189, 1129.
      Britton, L., et al. 1978. J. Bacteriol. 134, 229.
      Keele, B.B., et al. 1971. J. Biol. Chem. 246, 2875.
      McCord, J.M. and Fridovich, I. 1969. J. Biol. Chem. 244, 6049.
      Product Information
      CAS number9054-89-1
      Activity≥3000 units/mg dry weight
      Unit of DefinitionOne unit is defined as the amount of enzyme that will cause a 50% inhibition in the rate of reduction of cytochrome <i>c</i> at 25°C, pH 7.8.
      EC number1.15.1.1
      FormLyophilized solid
      PI4.95
      Quality LevelMQ100
      Applications
      Biological Information
      Concentration Label Please refer to vial label for lot-specific concentration
      Physicochemical Information
      ContaminantsCarbonic anhydrase: ≤30 units/mg dry weight
      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 Moisture Protect from moisture
      Do not freeze Ok to freeze
      Special InstructionsFollowing reconstitution, aliquot and freeze (-20°C).
      Packaging Information
      Transport Information
      Supplemental Information
      Specifications
      Global Trade Item Number
      Référence GTIN
      574594-50KU 04055977189582

      Documentation

      Superoxide Dismutase, Bovine Erythrocytes FDS

      Titre

      Fiche de données de sécurité des matériaux (FDS) 

      Superoxide Dismutase, Bovine Erythrocytes Certificats d'analyse

      TitreNuméro de lot
      574594

      Références bibliographiques

      Aperçu de la référence bibliographique
      Tilly, J.L. and Tilly, K.I. 1995. Endocrinology 136, 242.
      Sharonov, B.P. and Churilova, I.V. 1992. Biochem. Biophys. Res. Commun. 189, 1129.
      Britton, L., et al. 1978. J. Bacteriol. 134, 229.
      Keele, B.B., et al. 1971. J. Biol. Chem. 246, 2875.
      McCord, J.M. and Fridovich, I. 1969. J. Biol. Chem. 244, 6049.

      Brochure

      Titre
      Caspases and other Apoptosis Related Tools Brochure
      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.

      Revision12-September-2008 RFH
      SynonymsCu/Zn SOD
      DescriptionNative superoxide dismutase from bovine erythrocytes. Essential component of biological defense against toxic effects of oxygen. Catalyzes the dismutation of superoxide radicals to oxygen and H2O2.
      FormLyophilized solid
      Concentration Label Please refer to vial label for lot-specific concentration
      CAS number9054-89-1
      EC number1.15.1.1
      ContaminantsCarbonic anhydrase: ≤30 units/mg dry weight
      Activity≥3000 units/mg dry weight
      Unit definitionOne unit is defined as the amount of enzyme that will cause a 50% inhibition in the rate of reduction of cytochrome c at 25°C, pH 7.8.
      Solubility5 mg/mL in 50 mM potassium phosphate, 100 µM EDTA, pH 7.8, yields a clear pale blue solution.
      Storage Protect from moisture
      -20°C
      Do Not Freeze Ok to freeze
      Special InstructionsFollowing reconstitution, aliquot and freeze (-20°C).
      Toxicity Standard Handling
      ReferencesTilly, J.L. and Tilly, K.I. 1995. Endocrinology 136, 242.
      Sharonov, B.P. and Churilova, I.V. 1992. Biochem. Biophys. Res. Commun. 189, 1129.
      Britton, L., et al. 1978. J. Bacteriol. 134, 229.
      Keele, B.B., et al. 1971. J. Biol. Chem. 246, 2875.
      McCord, J.M. and Fridovich, I. 1969. J. Biol. Chem. 244, 6049.