Product Details
| Alternative Name: | Phosphatase and tensin homolog deleted on chromosome 10 |
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| MW: | ~48 kDa |
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| Source: | Produced in E. coli. Full length human PTEN (aa 1-403) is fused at the N-terminus to a His-tag. |
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| EC: | 3.1.3.67 / 3.1.3.16 / 3.1.3.48 |
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| UniProt ID: | P60484 |
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| 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. |
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| Purity: | ≥80% (SDS-PAGE) |
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| Purity Detail: | Purified by multi-step chromatography. |
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| Specific Activity: | ≥ 7 pmol/min/µg assayed by Ptdlns(3,4,5)P3 (Prod. No. BML-PH107) (60 µM) hydrolysis at 37°C |
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| 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. |
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| Shipping: | Dry Ice |
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| Long Term Storage: | -80°C |
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| Handling: | After opening, prepare aliquots, freeze in liquid nitrogen and store at -80°C. Avoid freeze/thaw cycles. |
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| 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. |
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| Regulatory Status: | RUO - Research Use Only |
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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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