539734 PTP, Yersinia enterocolitica, Recombinant, E. coli

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539734
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539734-2000U
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      Description
      Overview

      This product has been discontinued.



      Recombinant, 51 kDa catalytic domain of the Yersinia protein tyrosine phosphatase containing a C235R mutation and expressed in E. coli. Suitable for dephosphorylation of phosphotyrosine residues in proteins.

      Catalogue Number539734
      Brand Family Calbiochem®
      SynonymsYOP, Protein Tyrosine Phosphatase, Yersenia
      References
      ReferencesZhang, Z.Y., et al. 1992. J. Biol. Chem. 267, 23759.
      Gordon, J.A. 1991. Methods Enzymol. 201, 477.
      Guan, K. and Dixon, J.E. 1990. Science 249, 653.
      Product Information
      Activity≥50,000 units/ml
      Unit of DefinitionOne unit is defined as the amount of enzyme that will hydrolyze 1 nmol of <i>p</i>NPP per min at 30°C, pH 7.2.
      FormLiquid
      FormulationIn 100 mM NaCl, 50 mM HEPES, 5 mM DTT, 2 mM EDTA, 0.01% BRIJ® 35 Detergent, 50% glycerol, pH 7.0.
      Quality LevelMQ100
      Applications
      Biological Information
      Purity≥95% by SDS-PAGE
      Specific Activity≥50,000 units/mg
      Physicochemical Information
      ContaminantsProteases, serine/threonine phosphatases: none detected
      Dimensions
      Materials Information
      Toxicological Information
      Safety Information according to GHS
      Safety Information
      Product Usage Statements
      Storage and Shipping Information
      Ship Code Dry Ice Only
      Toxicity Standard Handling
      Storage ≤ -70°C
      Avoid freeze/thaw Avoid freeze/thaw
      Do not freeze Ok to freeze
      Special InstructionsFollowing initial thaw, aliquot and freeze (-70°C).
      Packaging Information
      Transport Information
      Supplemental Information
      Specifications

      Documentation

      PTP, Yersinia enterocolitica, Recombinant, E. coli SDS

      Title

      Safety Data Sheet (SDS) 

      PTP, Yersinia enterocolitica, Recombinant, E. coli Certificates of Analysis

      TitleLot Number
      539734

      References

      Reference overview
      Zhang, Z.Y., et al. 1992. J. Biol. Chem. 267, 23759.
      Gordon, J.A. 1991. Methods Enzymol. 201, 477.
      Guan, K. and Dixon, J.E. 1990. Science 249, 653.

      Brochure

      Title
      Protein Phosphatases Technical Bulletin

      Citations

      Title
    • Meyn, M.A, et al. 2005. Molecular Pharmacology 68, 1320.
    • 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.

      Revision08-September-2008 RFH
      SynonymsYOP, Protein Tyrosine Phosphatase, Yersenia
      DescriptionRecombinant, 51 kDa catalytic domain of the Yersinia protein tyrosine phosphatase containing a C235R mutation and expressed in E. coli. Suitable for dephosphorylation of phosphotyrosine residues in proteins
      FormLiquid
      FormulationIn 100 mM NaCl, 50 mM HEPES, 5 mM DTT, 2 mM EDTA, 0.01% BRIJ® 35 Detergent, 50% glycerol, pH 7.0.
      Recommended reaction conditions50 mM Tris-HCl, pH 7.2, 150 mM NaCl, 5 mM DTT, 2.5 mM Na2EDTA, and 100 µg/ml BSA. Incubate at 30°C. 2.5 units will typically remove >95% of phosphates from tyrosine residues in 0.1 nmol of protein in 30 min.
      Purity≥95% by SDS-PAGE
      ContaminantsProteases, serine/threonine phosphatases: none detected
      Specific activity≥50,000 units/mg
      Activity≥50,000 units/ml
      Unit definitionOne unit is defined as the amount of enzyme that will hydrolyze 1 nmol of pNPP per min at 30°C, pH 7.2.
      Storage ≤ -70°C
      Avoid freeze/thaw
      Do Not Freeze Ok to freeze
      Special InstructionsFollowing initial thaw, aliquot and freeze (-70°C).
      Toxicity Standard Handling
      ReferencesZhang, Z.Y., et al. 1992. J. Biol. Chem. 267, 23759.
      Gordon, J.A. 1991. Methods Enzymol. 201, 477.
      Guan, K. and Dixon, J.E. 1990. Science 249, 653.
      Citation
    • Meyn, M.A, et al. 2005. Molecular Pharmacology 68, 1320.