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Anti-PTEN Phospho Antibody EP229
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Also for PTEN (NM_000314)
|A phospho-specific peptide corresponding to residues surrounding Threonine 366 and Serine 370 of human PTEN was used as an immunogen. The antibody only detects PTEN phosphorylated on T366 or S370.|
||ICC: 1:100 - 250, IHC: 1:100 - 250, IP: 1:50, WB: 1:1,000 - 10,000,
|Store at -20 C. Buffer: 50 mM Tris-Glycine (pH 7.4), 0.15 M NaCl, 40% Glycerol, 0.01% sodium azide and 0.05% BSA. Stable for 12 months from date of receipt.|
|Homo sapiens phosphatase and tensin homolog (PTEN)|
|10q23del; BZS; DEC; GLM2; MHAM; MMAC1; PTEN1; TEP1|
|PTEN is a protein tyrosine phosphatase that acts as a tumor suppressor, as a lipid phosphatase that dephosphorylates the D3 position of phosphatidylinositol 3,4,5-trisphosphate and as an antagonist of the PI3k/AKT signaling pathway (1-3). PTEN structural domains includes an N-terminal phosphatase domain, a lipid binding C2 domain and a 50-amino acid C-terminal tail that contains a PDZ biding sequence. Phosphorylation of the tail suppresses the activity of PTEN by controlling its recruitment into the PTEN-associated complex (4). PTEN is phosphorylated in vitro on Threonine 366 and Serine 370 by glycogen synthase kindase 3 (GSK3) and casein kinase 2 (CK2) respectively. Prior phosphorylation of PTEN at Serine 370 by CK2 strongly increased its phosphorylation at Threonine 366 by GSK3, suggesting that the two may synergize. Generally, phosphorylation in the C-terminal tail of PTEN is thought to enhance stability and to decrease membrane localization and activity. However, phosphorylation at Threonine 366 is linked to destabilization of PTEN (5). |
Senescence and Autophagy
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A. Western blot analysis on HeLa cell lysates using anti-Phospho-PTEN (pT366/S370) RabMAb .
B. Immunohistochemical analysis of paraffin-embedded human breast ductal carcinoma using anti-Phospho-PTEN RabMAb .