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PTEN Antibody (N-term) Blocking Peptide

Synthetic peptide

Product Information
Primary Accession P60484
Clone Names 3110603
Peptide ID 3110603
Additional Information
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
Target/Specificity The synthetic peptide sequence used to generate the antibody AP8436a was selected from the N-term region of human PTEN. A 10 to 100 fold molar excess to antibody is recommended. Precise conditions should be optimized for a particular assay.
Format The synthetic peptide was lyophilized with 100% acetonitrile and is supplied as a powder. Reconstitute with 0.1 ml deionized water for a final concentration of 1 mg/ml.
StorageMaintain refrigerated at 2-8°C for up to 6 months. For long term storage store at -20°C.
PrecautionsThis product is for research use only. Not for use in diagnostic or therapeutic procedures.
Protein Information
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. 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.
Research Areas
Citations (0)

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PTEN, (phosphatase and tensin homolog deleted on chromosome 10), also known as MMAC1 (mutated in multiple advanced cancers 1), is a tumor suppressor implicated in a large number of human tumors. The PTEN phosphatase incorporates the catalytic motif (HCXXGXXRS/T) that is a signature of the protein tyrosine phosphatase family. Recombinant human PTEN is a dual phosphatase with ability to dephosphorylate both tyrosine and serine/threonine residues. PTEN functions primarily as a lipid phosphatase to regulate signal transduction pathways, with a primary target identified as phosphatidylinositol 3,4,5 trisphosphate. In addition, PTEN presents weak tyrosine phosphatase activity, which may downregulate signaling pathways involving focal adhesion kinase or Shc. PTEN negatively regulates activation of the serine/threonine kinase Akt/PKB by blocking its phosphorylation, thereby inhibiting the PI 3 kinase Akt signaling pathway, which is important for cell survival. In vivo, the majority of PTEN missense mutations detected in tumor specimens target the phosphatase domain and cause a loss in PTEN phosphatase activity. Mutations in PTEN are associated with several common cancers including prostate, brain and breast cancer, and with Cowden's disease, an autosomal dominant disorder conferring susceptibility to benign and malignant tumors. Germline mutations of PTEN are also linked Lhermitte-Duclos disease and Bannayan-Zonana syndrome. Mutations of PTEN occur in 60 to 80% of prostate cancers. PTEN is also essential for embryonic development.

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$ 80.00
Cat# BP8436a
(40 western blots)
Availability: In Stock
Bulk Size
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