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PTEN (human), (recombinant) (His-tag)

BML-SE402-0010 10 µg 531.00 USD
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Product Details

Alternative Name:Phosphatase and tensin homolog deleted on chromosome 10
MW:~48 kDa
Source:Produced in E. coli. Full length human PTEN (aa 1-403) is fused at the N-terminus to a His-tag.
EC: / /
UniProt ID:P60484
Formulation:Liquid. In 50mM TRIS-HCl, pH 8.0, containing 150mM sodium chloride, 5mM DTT, 0.03% Brij 35, 0.1mM EDTA and 20% glycerol.
Purity:≥80% (SDS-PAGE)
Purity Detail:Purified by multi-step chromatography.
Specific Activity:≥ 7 pmol/min/µg assayed by Ptdlns(3,4,5)P3 (Prod. No. BML-PH107) (60 µM) hydrolysis at 37°C
Application Notes:Can be used to study regulation and kinetics of PTEN, screen for PTEN inhibitors or activators or as positive control for Western blots.
Shipping:Dry Ice
Long Term Storage:-80°C
Handling:After opening, prepare aliquots, freeze in liquid nitrogen and store at -80°C. Avoid freeze/thaw cycles.
Scientific Background:PTEN (phosphatase and tensin homologue deleted on chromosome 10, MMAC) is a lipid phosphatase which can also act as a tyrosine, serine and threonine protein phosphatase. It is specific for acidic substrates such as phosphatidylinositol(3,4,5)-trisphosphate, which is its main biological substrate that mediates growth factor-induced activation of intracellular signalling through the serine-threonine kinase Akt. The tumor suppressor gene, PTEN, also known as MMAC1 or TEP1, has been isolated from a locus on chromosome 1Oq23; this protein is deleted or mutated in a large number of tumors. Germline mutations of PTEN have been identified in Cowden disease, Lhermitte-Duclos disease, and Bannayan-Zonana syndrome.
Regulatory Status:RUO - Research Use Only

Product Literature References

Evidence against Stable Protein S-Nitrosylation as a Widespread Mechanism of Post-translational Regulation: K. Wolhuter, et al.; Mol. Cell 69, 438 (2018), Abstract; Full Text

General Literature References

PTEN regulatory functions in tumor suppression and cell biology: E.C. Chu & A.S. Tarnawski; Med. Sci. Monit. 10, RA235 (2004), Abstract;
The biology and clinical relevance of the PTEN tumor suppressor pathway: I. Sansal & W.R. Sellers; J. Clin. Oncol. 22, 2954 (2004), Abstract;
Allosteric activation of PTEN phosphatase by phosphatidylinositol 4,5-bisphosphate: R.B. Campbell, et al.; J. Biol. Chem. 278, 33617 (2003), Abstract; Full Text
PTEN: D. Stokoe; Curr. Biol. 11, R502 (2001), Abstract;
Functional evaluation of PTEN missense mutations using in vitro phosphoinositide phosphatase assay: S.Y. Han, et al.; Cancer Res. 60, 3147 (2000), Abstract; Full Text
Crystal structure of the PTEN tumor suppressor: implications for its phosphoinositide phosphatase activity and membrane association: J.O. Lee, et al.; Cell 99, 323 (1999), Abstract;
The tumor suppressor, PTEN/MMAC1, dephosphorylates the lipid second messenger, phosphatidylinositol 3,4,5-trisphosphate: T. Maehama & J.E. Dixon; J. Biol. Chem. 273, 13375 (1998), Abstract; Full Text

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