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598502 Thioredoxin Reductase, Yeast, Recombinant, E. coli

MSDS (material safety data sheet) or SDS, CoA and CoQ, dossiers, brochures and other available documents.

Synonyms: ryNTR

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598502
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Overview

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598502-100UGCN
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      		 Plastic ampoule 100 μg
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      Description
      OverviewRecombinant, yeast thioredoxin reductase expressed in E. coli. Yeast thioredoxin reductase is a flavoprotein that has no selenocysteine (SeCys). It catalyzes the NADPH-dependent reduction of thioredoxin as well as other endogenous and exogenous proteins. Plays an important role in many aspects of cell function, including protection against oxidative stress/injury, cell growth and transformation, and the recycling of ascorbate from its oxidized form.
      Catalogue Number598502
      Brand Family Calbiochem®
      SynonymsryNTR
      References
      ReferencesMustacich, D. and Powis, G. 2000. Biochem. J. 346, 1.
      Wang, P.F., et al. 1998. Biochemistry 37, 16378.
      Holmgren, A., 1979. J. Biol. Chem. 254, 9627.
      Product Information
      Unit of DefinitionOne unit is defined as the amount of enzyme that will cause an absorbance change of 1 at 412 nm using 200 µM NADPH and 5 mM DTNB, per min at 25°C, pH 7.0.
      FormLyophilized solid
      FormulationLyophilized from 150 mM NaCl, 20 mM phosphate buffer, pH 7.4.
      Quality LevelMQ100
      Applications
      Biological Information
      Purity≥95% by SDS-PAGE
      Specific Activity≥5 units/mg protein
      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 -20°C
      Do not freeze Ok to freeze
      Special InstructionsFollowing reconstitution, aliquot and freeze (-70°C). Stock solutions are stable for 1 month at 4°C or 3 months at -70°C.
      Packaging Information
      Transport Information
      Supplemental Information
      Specifications
      Global Trade Item Number
      Catalogue Number GTIN
      598502-100UGCN 04055977189186

      Documentation

      Thioredoxin Reductase, Yeast, Recombinant, E. coli SDS

      Title

      Safety Data Sheet (SDS) 

      Thioredoxin Reductase, Yeast, Recombinant, E. coli Certificates of Analysis

      TitleLot Number
      598502

      References

      Reference overview
      Mustacich, D. and Powis, G. 2000. Biochem. J. 346, 1.
      Wang, P.F., et al. 1998. Biochemistry 37, 16378.
      Holmgren, A., 1979. J. Biol. Chem. 254, 9627.
      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.

      Revision10-June-2008 JSW
      SynonymsryNTR
      DescriptionRecombinant, yeast thioredoxin reductase expressed in E. coli. Yeast thioredoxin reductase is a flavoprotein that has no selenocysteine (SeCys). It catalyzes the NADPH-dependent reduction of thioredoxin as well as other endogenous and exogenous proteins. Plays an important role in many aspects of cell function, including protection against oxidative stress/injury, cell growth and transformation, and the recycling of ascorbate from its oxidized form.
      FormLyophilized solid
      FormulationLyophilized from 150 mM NaCl, 20 mM phosphate buffer, pH 7.4.
      Purity≥95% by SDS-PAGE
      Specific activity≥5 units/mg protein
      Unit definitionOne unit is defined as the amount of enzyme that will cause an absorbance change of 1 at 412 nm using 200 µM NADPH and 5 mM DTNB, per min at 25°C, pH 7.0.
      SolubilityAqueous buffers, pH 7.0
      Storage -20°C
      Do Not Freeze Ok to freeze
      Special InstructionsFollowing reconstitution, aliquot and freeze (-70°C). Stock solutions are stable for 1 month at 4°C or 3 months at -70°C.
      Toxicity Standard Handling
      ReferencesMustacich, D. and Powis, G. 2000. Biochem. J. 346, 1.
      Wang, P.F., et al. 1998. Biochemistry 37, 16378.
      Holmgren, A., 1979. J. Biol. Chem. 254, 9627.