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PTEN Antibody (Center S294) Blocking Peptide
Synthetic peptide
- SPECIFICATION
- CITATIONS
- PROTOCOLS
- BACKGROUND
| Primary Accession | P60484 |
|---|---|
| Clone Names | 111026140 |
| Gene ID | 5728 |
|---|---|
| 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 |
| Format | Peptides are lyophilized in a solid powder format. Peptides can be reconstituted in solution using the appropriate buffer as needed. |
| Storage | Maintain refrigerated at 2-8°C for up to 6 months. For long term storage store at -20°C. |
| Precautions | This product is for research use only. Not for use in diagnostic or therapeutic procedures. |
| Name | PTEN |
|---|---|
| Synonyms | MMAC1, TEP1 |
| 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, PubMed:16824732). 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 (PubMed:18716620). XIAP/BIRC4 promotes its nuclear localization (PubMed:19473982). |
| 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.
Background
This gene was identified as a tumor suppressor that ismutated in a large number of cancers at high frequency. The proteinencoded this gene is a phosphatidylinositol-3,4,5-trisphosphate3-phosphatase. It contains a tensin like domain as well as acatalytic domain similar to that of the dual specificity proteintyrosine phosphatases. Unlike most of the protein tyrosinephosphatases, this protein preferentially dephosphorylatesphosphoinositide substrates. It negatively regulates intracellularlevels of phosphatidylinositol-3,4,5-trisphosphate in cells andfunctions as a tumor suppressor by negatively regulating AKT/PKBsignaling pathway.
References
Miletic, A.V., et al. J. Exp. Med. 207(11):2407-2420(2010)Kini, V., et al. J. Biol. Chem. 285(43):33082-33091(2010)Shimada, M., et al. Hum. Genet. 128(4):433-441(2010)Molina, J.R., et al. Cancer Res. 70(17):6697-6703(2010)Iliopoulos, D., et al. Mol. Cell 39(4):493-506(2010)
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