PHOENIX SECRETOMICS | 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. May be a negative regulator of insulin signaling and glucose metabolism in adipose tissue. | ||
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| Model for the inhibition of PI 3-kinase signalling by PTEN and SHIP at the plasma membrane. Nick R. Leslie and C. Peter Downes. Biochem J. 2004 August 15; 382(Pt 1): 1–11. | ||
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| The 403-amino-acid PTEN protein is represented. The N-terminal phosphatase domain (amino acids 7–185) and the C2 domain (186–351) are both required for enzymic activity. The catalytic cysteine residue (Cys-124) is represented by a large encircled letter C, and Cys-71 by a smaller letter c. These residues form a reversible disulphide bond when the enzyme becomes oxidized. The N-terminal PtdIns(4,5)P2 binding motif is shown at the N-terminal end of the phosphatase domain, although it is uncertain whether in cells this motif responds to PtdIns(4,5)P2, or perhaps another more abundant acidic lipid such as phosphatidylserine. The extreme C-terminal PDZ binding sequence is also shown, and although it is represented as a small region, the extent of further sequences required for optimal specificity and affinity of binding is not known. The phosphorylation sites in the C-terminal tail are represented by a circled letter P.
Nick R. Leslie and C. Peter Downes. Biochem J. 2004 August 15; 382(Pt 1): 1–11. |
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| Immunofluorescence staining of methanol-fixed HeLa cells showing cytoplasmic localization PTEN C-Terminal Antibody. | Western blot analysis of PTEN expression in A-431 (A) and KNRK (B) whole cell lysates PTEN C-Terminal Antibody. | Western blot analysis of PTEN expression in A-431 (A), KNRK (B), HeLa (C) and MDCK (D) whole cell lysates PTEN N-Terminal Antibody. |
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Immunoperoxidase staining of formalin-fixed, paraffin-embedded human breast carcinoma tissue showing cytoplasmic staining by anti-phosphorylated PTEN (Ser370) Antibody. |
Western blot analysis of phosphorylated PTEN expression in untreated (A) and vanadate-treated (B) A-431 whole cell lysates by anti-phosphorylated PTEN (Ser370) Antibody. | |
| Antibody Name | Application | Antibody Type | Specices | Host | Catalog No.: | Size |
Price |
| PTEN C-Terminal Antibody | IF (1: 100), WB (1:200-500) | Monoclonal | h, r | mouse | PS001-51-MAG-01 | 100 ug |
360 |
| PTEN C-Terminal Antibody | WB (1:200) | Polyclonal | h, r, m | rabbit | PS001-51-AG-01 | 100 ug |
360 |
| PTEN N-Terminal Antibody | WB (1:200) | Polyclonal | h, r, m | goat | PS001-51-AG-02 | 100 ug |
360 |
| phosphorylated PTEN (Ser370) Antibody | WB (1:200), IHC (1:50-500) | Polyclonal | h | rabbit | PS001-51-AG-03 | 100 ug |
360 |