Anti-PTEN Antibody
433.5 EUR
In Stock
quantity
Produktdetaljer
Katalognummer: 992 - ER1902-33
Produktkategori: Företag och industri > Vetenskap och laboratorium
Gentaur
Storlek: 100ul
Parameters
| Additional information | Synthetic peptide within human PTEN aa 350-403. |
|---|---|
| Storage and shipping | Store at +4℃ after thawing. Aliquot store at -20℃. Avoid repeated freeze / thaw cycles. |
ER1902-27
Anti-PTEN Antibody
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.
433.5 €
ER1902-33
Anti-PTEN Antibody
Tumor suppressor. Acts as a dual-specificity protein phosphatase, dephosphorylating tyrosine-, serine- and threonine-phosphorylated proteins. Also acts as a lipid phosphatase. 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.
433.5 €
ER1706-51
Anti-PTEN Antibody
As human tumors progress to advanced stages, one genetic alteration that occurs at high frequency is a loss of heterozygosity (LOH) at chromosome 10q23. Mapping of homozygous deletions on this chromosome led to the isolation of the PTEN gene, also designated MMAC1 (for mutated in multiple advanced cancers) and TEP1. This candidate tumor suppressor gene exhibits a high frequency of mutations in human glioblastomas and is also mutated in other cancers, including sporadic brain, breast, kidney and prostate cancers. PTEN has been associated with Cowden disease, an autosomal dominant cancer predisposition syndrome. The PTEN gene product is a putative protein tyrosine phosphatase that is localized to the cytoplasm and shares extensive homology with the cytoskeletal proteins tensin and auxilin. Gene transfer studies have indicated that the phosphatase domain of PTEN is essential for growth suppression of glioma cells.
433.5 €
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