|Application ||WB, IF, E, IP|
|Other Accession||P60484, 5728|
|Calculated MW||47166 Da|
|Application Notes||PTEN antibody can be used for the detection of PTEN by Western blot at 1 to 2 μg/mL. For immunofluorescence start at 2 μg/mL.|
|Other Names||PTEN Antibody: BZS, DEC, CWS1, GLM2, MHAM, TEP1, MMAC1, PTEN1, 10q23del, Phosphatidylinositol 3, 4, 5-trisphosphate 3-phosphatase and dual-specificity protein phosphatase PTEN, Mutated in multiple advanced cancers 1, phosphatase and tensin homolog|
|Target/Specificity||PTEN antibody was raised against a 15 amino acid synthetic peptide from near the amino terminus of human PTEN.|
The immunogen is located within the first 50 amino acids of PTEN.
|Reconstitution & Storage||PTEN antibody can be stored at 4℃ for three months and -20℃, stable for up to one year. As with all antibodies care should be taken to avoid repeated freeze thaw cycles. Antibodies should not be exposed to prolonged high temperatures.|
|Precautions||PTEN Antibody is for research use only and not for use in diagnostic or therapeutic procedures.|
|Function||Tumor suppressor. Acts as a dual-specificity protein phosphatase, dephosphorylating tyrosine-, serine- and threonine- phosphorylated proteins. Also acts as a lipid phosphatase, removing the phosphate in the D3 position of the inositol ring from phosphatidylinositol 3,4,5-trisphosphate, phosphatidylinositol 3,4-diphosphate, phosphatidylinositol 3- phosphate and inositol 1,3,4,5-tetrakisphosphate with order of substrate preference in vitro PtdIns(3,4,5)P3 > PtdIns(3,4)P2 > PtdIns3P > Ins(1,3,4,5)P4 (PubMed:26504226). The lipid phosphatase activity is critical for its tumor suppressor function. Antagonizes the PI3K-AKT/PKB signaling pathway by dephosphorylating phosphoinositides and thereby modulating cell cycle progression and cell survival. The unphosphorylated form cooperates with AIP1 to suppress AKT1 activation. Dephosphorylates tyrosine-phosphorylated focal adhesion kinase and inhibits cell migration and integrin-mediated cell spreading and focal adhesion formation. Plays a role as a key modulator of the AKT-mTOR signaling pathway controlling the tempo of the process of newborn neurons integration during adult neurogenesis, including correct neuron positioning, dendritic development and synapse formation. May be a negative regulator of insulin signaling and glucose metabolism in adipose tissue. The nuclear monoubiquitinated form possesses greater apoptotic potential, whereas the cytoplasmic nonubiquitinated form induces less tumor suppressive ability. In motile cells, suppresses the formation of lateral pseudopods and thereby promotes cell polarization and directed movement.|
|Cellular Location||Cytoplasm. Nucleus. Nucleus, PML body. Note=Monoubiquitinated form is nuclear. Nonubiquitinated form is cytoplasmic. Colocalized with PML and USP7 in PML nuclear bodies XIAP/BIRC4 promotes its nuclear localization|
|Tissue Location||Expressed at a relatively high level in all adult tissues, including heart, brain, placenta, lung, liver, muscle, kidney and pancreas.|
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Provided below are standard protocols that you may find useful for product applications.
PTEN Antibody: PTEN (phosphatase and tensin homologue deleted on chromosome ten) is a dual-specificity phosphatase (with both protein and lipid phosphatase activity) first identified as a tumor suppressor gene. PTEN indirectly activates the AKT/PI3K pathway, an important signaling pathway for cell growth and proliferation by keeping levels of the second messenger PIP3 low, thereby preventing phosphoinositide-dependent kinase-1 (PDK-1) from phosphorylating and activating AKT. Expression of wild-type PTEN causes growth arrest in many cancer cell lines, but expression of a PTEN protein containing a mutation that blocks its lipid phosphatase activity failed to suppress growth of glioma cell lines suggesting that the tumor suppressive effect of PTEN is mediated solely by its lipid phosphatase activity. Other activities include the inhibition of insulin stimulated MAPK activation by blocking the insulin-receptor substrate (IRS)-1 phosphorylation and assembly of the IRS-1/Grb2/Sos complex.
Li J, Yen C, Liaw D, et al. PTEN, a putative protein tyrosine phosphatase gene mutated in human brain, breast, and prostate cancer. Science1997; 275:1943-7.
Steck PA, Pershouse MA, Jasser SA, et al. Identification of a candidate tumor suppressor gene, MMAC1, a chromosome 10q23.3 that is mutated in multiple advanced cancers. Nat. Genet.1997; 15:356-62.
Wu X, Senechal K, Neshat MS, et al. The PTEN/MMAC1 tumor suppressor phosphatase functions as a negative regulator of the phosphoinositide 3-kinase/Akt pathway. Proc. Natl. Acad. Sci. USA1998; 95:15587-91.
Myers MP, Pass I, Batty IH, et al. The lipid phosphatase activity of PTEN is critical for its tumor suppressor function. Proc. Natl. Acad. Sci. USA1998; 95:13513-8.
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