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539734 PTP, Yersinia enterocolitica, Recombinant, E. coli

PTP, Yersinia enterocolitica, Recombinant, E. coli MSDS (material safety data sheet) or SDS, CoA and CoQ, dossiers, brochures and other available documents.

Synonyms: YOP, Protein Tyrosine Phosphatase, Yersenia

539734
  
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Áttekintés

Replacement Information
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
Global Trade Item Number
Katalógusszám GTIN
539734 0

Documentation

PTP, Yersinia enterocolitica, Recombinant, E. coli MSDS

Title

Safety Data Sheet (SDS) 

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

TitleLot Number
539734

References

Hivatkozások áttekintése
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

Titulus
  • 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 Avoid freeze/thaw
    ≤ -70°C
    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.
    		•