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354406 Glutaredoxin-S2, E. coli

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354406
  
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      Aperçu

      Replacement Information
      Description
      OverviewNative glutaredoxin-S2 isolated from E. coli. Glutaredoxin functions as a glutathione-dependent hydrogen donor for ribonucleotide reductase. It is useful as a general disulfide reductant for the in vitro study of protein folding mechanisms and has been demonstrated to work in conjunction with protein disulfide isomerase to enhance refolding of scrambled RNase A and RNase T1.
      Catalogue Number354406
      Brand Family Calbiochem®
      SynonymsGrx1
      References
      ReferencesRuoppolo, M., et al. 1997. Biochemistry 36, 12259.
      Sun, C., et al. 1997. Protein Sci. 6, 383.
      Prinz, W.A., et al. 1997. J. Biol. Chem. 272, 15661.
      Holmgren, A. and Alund, F. 1995 Methods Enzymol. 252, 283.
      Hoog, J.O., et al. 1986. Gene 43, 13.
      Product Information
      Unit of DefinitionUnits are defined using a standard HED assay.
      FormLyophilized
      FormulationLyophilized from 0.5% NH₄HCO₃.
      Quality LevelMQ100
      Applications
      ApplicationGlutaredoxin-S2, E. coli, acts as a glutathione-dependent hydrogen donor for ribonucleotide reductase. Useful as a general disulfide reductant for the in vitro study of protein folding mechanisms.
      Biological Information
      Specific Activity≥175 µmole NADPH oxidized/min/mg
      Physicochemical Information
      Dimensions
      Materials Information
      Toxicological Information
      Safety Information according to GHS
      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 Ok to freeze
      Special InstructionsFollowing reconstitution, aliquot and freeze (-20°C). Stock solutions are stable for up to 2 months at -20°C.
      Packaging Information
      Transport Information
      Supplemental Information
      Specifications
      Global Trade Item Number
      Référence GTIN
      354406 0

      Documentation

      Glutaredoxin-S2, E. coli FDS

      Titre

      Fiche de données de sécurité des matériaux (FDS) 

      Glutaredoxin-S2, E. coli Certificats d'analyse

      TitreNuméro de lot
      354406

      Références bibliographiques

      Aperçu de la référence bibliographique
      Ruoppolo, M., et al. 1997. Biochemistry 36, 12259.
      Sun, C., et al. 1997. Protein Sci. 6, 383.
      Prinz, W.A., et al. 1997. J. Biol. Chem. 272, 15661.
      Holmgren, A. and Alund, F. 1995 Methods Enzymol. 252, 283.
      Hoog, J.O., et al. 1986. Gene 43, 13.
      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.

      Revision01-July-2008 RFH
      SynonymsGrx1
      DescriptionNative glutaredoxin-S2 isolated from E. coli. Glutaredoxin functions as a glutathione-dependent hydrogen donor for ribonucleotide reductase. It is useful as a general disulfide reductant for the in vitro study of protein folding mechanisms and has been demonstrated to work in conjunction with protein disulfide isomerase to enhance refolding of scrambled RNase A and RNase T1.
      FormLyophilized
      FormulationLyophilized from 0.5% NH₄HCO₃.
      Specific activity≥175 µmole NADPH oxidized/min/mg
      Unit definitionUnits are defined using a standard HED assay.
      SolubilityReconstitute in 1 ml 50 mM Tris-HCl, 1 mM EDTA, pH 7.5 to yield a final concentration of 1 mg/ml.
      Storage +2°C to +8°C
      Do Not Freeze Ok to freeze
      Special InstructionsFollowing reconstitution, aliquot and freeze (-20°C). Stock solutions are stable for up to 2 months at -20°C.
      Toxicity Standard Handling
      ReferencesRuoppolo, M., et al. 1997. Biochemistry 36, 12259.
      Sun, C., et al. 1997. Protein Sci. 6, 383.
      Prinz, W.A., et al. 1997. J. Biol. Chem. 272, 15661.
      Holmgren, A. and Alund, F. 1995 Methods Enzymol. 252, 283.
      Hoog, J.O., et al. 1986. Gene 43, 13.