anti-PTEN, mAb (22F2)

CHF 315.00
In stock
YIF-LF-MA0287100 µlCHF 315.00
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Product Details
Synonyms PTEN; MMAC1; EC=; EC=; EC=; Phosphatase and Tensin Homolog; Mutated in Multiple Advanced Cancers 1; Phosphatidylinositol 3;4;5-Trisphosphate 3-Phosphatase and Dual-Specificity Protein Phosphatase PTEN
Product Type Monoclonal Antibody
Clone 22F2
Isotype Mouse IgG1 κ
Immunogen/Antigen Recombinant human His-PTEN protein purified from E. coli.

Western Blot (1:2,000)

Crossreactivity Human
Purity Detail Ammonium sulfate precipitation.
Formulation Liquid. HEPES with 0.15M NaCl, 0.01% BSA, 0.03% sodium azide, and 50% glycerol.
Isotype Negative Control

Mouse IgG1 Isotype Control

Other Product Data

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Our product description may differ slightly from the original manufacturers product datasheet.

Declaration Manufactured by AbFrontier
Shipping and Handling
Shipping BLUE ICE
Short Term Storage +4°C
Long Term Storage -20°C
Use/Stability Stable for at least 1 year after receipt when stored at -20°C.
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Product Specification Sheet
Datasheet Download PDF

PTEN acts as a phosphatase to dephosphorylate phosphatidylinositol (3,4,5)-trisphosphate (PtdIns (3,4,5)P3). The product of this enzymatic reaction is PtdIns(4,5)P2. This dephosphorylation is important because it results in inhibition of the AKT signaling pathway. PTEN is a 403 amino acid protein, and a member of the large PTP (protein tyrosine phosphatase) family. PTEN crystal structure revealed that the N-terminal phosphatase domain is followed by a tightly associated C-terminal C2 domain. These two domains together form a minimal catalytic unit. The phosphatase domain contains the active site which carries out the enzymatic function of the protein, whilst the C2 domain allows PTEN to bind to the phospholipid membrane. PTEN is one of the most commonly lost tumour suppressors in human cancer, and its deregulation is also implicated in several other diseases. Hereditary mutation of PTEN causes tumor-susceptibility diseases such as Cowden disease. 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.

Product References

1) Hamada K et al. (2005) Genes Dev 19 (17): 2054–65. (General)
2) Leslie NR and Downes CP, (2004) Biochem J 382 (Pt 1) : 1–11. (General)
3) Li J et al. (1997) Science 275 (5308): 1943–1947. (General)

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