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539510 PP2A₂, Bovine Kidney

PP2A₂, Bovine Kidney MSDS (material safety data sheet) or SDS, CoA and CoQ, dossiers, brochures and other available documents.

Synonyms: Protein Phosphatase 2A₂

539510
  
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Přehled

Replacement Information
Description
OverviewNative, PP2A2 from bovine kidney. A divalent cation-independent protein serine/threonine phosphatase involved in the control of numerous cellular processes. Has a catalytic subunit of 36 kDa and a regulatory subunit of 60 kDa. Transient phosphorylation of the catalytic subunit on threonine or tyrosine residues has been reported to inactivate PP2A2. Inhibits nuclear telomerase activity in human breast cancer cells.

This product has been discontinued.
Catalogue Number539510
Brand Family Calbiochem®
SynonymsProtein Phosphatase 2A₂
References
ReferencesLi, H., et al. 1997. J. Biol. Chem. 272, 16729.
Guo, H. and Damuni, Z. 1993. Proc. Natl. Acad. Sci. USA 90, 2500.
Hendrix, P., et al. 1993. J. Biol. Chem. 268, 15267.
Amick, G.D., et al. 1992. Biochem. J. 287, 1019.
Chen, J., et al. 1992. Science 257, 1261.
Cohen, P., et al. 1990. Trends Biochem. Sci. 15, 98.
Damuni, Z., et al. 1989. J. Biol. Chem. 264, 6412.
Product Information
Unit of DefinitionOne unit is defined as the amount of enzyme that will release 1.0 nmol of [³²P]P<sub>i</sub> from ³²P-labeled phosphorylase per min at 30°C, pH 7.0.
EC number3.1.3.16
FormLiquid
FormulationIn 25 mM Tris-HCl, 14 mM βME, 1 mM benzamidine, 100 µM EDTA, 100 µM PMSF, 50% glycerol, pH 7.0.
Applications
Biological Information
Purity≥90% by SDS-PAGE
Specific Activity≥750 units/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 -20°C
Do not freeze Ok to freeze
Special InstructionsFollowing initial thaw, aliquot and freeze (-20°C).
Packaging Information
Transport Information
Supplemental Information
Specifications
Global Trade Item Number
Katalogové číslo GTIN
539510 0

Documentation

PP2A₂, Bovine Kidney MSDS

Title

Safety Data Sheet (SDS) 

PP2A₂, Bovine Kidney Certificates of Analysis

TitleLot Number
539510

References

Přehled odkazů
Li, H., et al. 1997. J. Biol. Chem. 272, 16729.
Guo, H. and Damuni, Z. 1993. Proc. Natl. Acad. Sci. USA 90, 2500.
Hendrix, P., et al. 1993. J. Biol. Chem. 268, 15267.
Amick, G.D., et al. 1992. Biochem. J. 287, 1019.
Chen, J., et al. 1992. Science 257, 1261.
Cohen, P., et al. 1990. Trends Biochem. Sci. 15, 98.
Damuni, Z., et al. 1989. J. Biol. Chem. 264, 6412.

Brochure

Title
Protein Phosphatases Technical Bulletin
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.

Revision05-September-2008 RFH
SynonymsProtein Phosphatase 2A₂
DescriptionNative, PP2A2 from bovine kidney. A divalent cation-independent protein serine/threonine phosphatase involved in the control of numerous cellular processes. Has a catalytic subunit of 36 kDa and a regulatory subunit of 60 kDa. Transient phosphorylation of the catalytic subunit on threonine or tyrosine residues has been reported to inactivate PP2A2. Inhibits nuclear telomerase activity in human breast cancer cells.
FormLiquid
FormulationIn 25 mM Tris-HCl, 14 mM βME, 1 mM benzamidine, 100 µM EDTA, 100 µM PMSF, 50% glycerol, pH 7.0.
EC number3.1.3.16
Purity≥90% by SDS-PAGE
Specific activity≥750 units/mg
Unit definitionOne unit is defined as the amount of enzyme that will release 1.0 nmol of [³²P]Pi from ³²P-labeled phosphorylase per min at 30°C, pH 7.0.
Storage -20°C
Do Not Freeze Ok to freeze
Special InstructionsFollowing initial thaw, aliquot and freeze (-20°C).
Toxicity Standard Handling
ReferencesLi, H., et al. 1997. J. Biol. Chem. 272, 16729.
Guo, H. and Damuni, Z. 1993. Proc. Natl. Acad. Sci. USA 90, 2500.
Hendrix, P., et al. 1993. J. Biol. Chem. 268, 15267.
Amick, G.D., et al. 1992. Biochem. J. 287, 1019.
Chen, J., et al. 1992. Science 257, 1261.
Cohen, P., et al. 1990. Trends Biochem. Sci. 15, 98.
Damuni, Z., et al. 1989. J. Biol. Chem. 264, 6412.