|Application ||IHC, WB|
|Calculated MW||47166 Da|
|Other Names||Phosphatidylinositol 3, 5-trisphosphate 3-phosphatase and dual-specificity protein phosphatase PTEN, Mutated in multiple advanced cancers 1, Phosphatase and tensin homolog, PTEN, MMAC1, TEP1|
|Target/Specificity||A phospho-specific peptide corresponding to residues surrounding Threonine 366 and Serine 370 of human PTEN was used as an immunogen. The antibody only detects PTEN phosphorylated on T366 or S370.|
|Format||50 mM Tris-Glycine (pH 7.4), 0.15 M NaCl, 40% Glycerol, 0.01% sodium azide and 0.05% BSA.|
|Storage||Maintain refrigerated at 2-8°C for up to 6 months. For long term storage store at -20°C in small aliquots to prevent freeze-thaw cycles.|
|Precautions||PTEN Antibody Phospho (pT366/pS370) 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 is a protein tyrosine phosphatase that acts as a tumor suppressor, as a lipid phosphatase that dephosphorylates the D3 position of phosphatidylinositol 3,4,5-trisphosphate and as an antagonist of the PI3k/AKT signaling pathway (1-3). PTEN structural domains includes an N-terminal phosphatase domain, a lipid binding C2 domain and a 50-amino acid C-terminal tail that contains a PDZ biding sequence. Phosphorylation of the tail suppresses the activity of PTEN by controlling its recruitment into the PTEN-associated complex (4). PTEN is phosphorylated in vitro on Threonine 366 and Serine 370 by glycogen synthase kindase 3 (GSK3) and casein kinase 2 (CK2) respectively. Prior phosphorylation of PTEN at Serine 370 by CK2 strongly increased its phosphorylation at Threonine 366 by GSK3, suggesting that the two may synergize. Generally, phosphorylation in the C-terminal tail of PTEN is thought to enhance stability and to decrease membrane localization and activity. However, phosphorylation at Threonine 366 is linked to destabilization of PTEN (5).
1. Vazquez, et al. Biochim. Biophys. Acta 1470, M21-M35, 2000
2. Maehama, T., et al. J. Biol. Chem. 273, 13375-13378, 1998
3. Maehama, et al. Annu. Rev. Biochem. 70, 247-279, 2001
4. Vazquez, et al. J. Biol. Chem., Vol. 276, Issue 52, 48627-48630, 2001
5. Tamguney, et al. J of Cell Science 120, 4071-4079, 2007
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