PTEN Antibody

• Western blot

  

  Western blot analysis using PTEN mouse mAb against HeLa (1) and NIH/3T3 (2) cell lysate.

• Immunofluorescence

  

  Confocal immunofluorescence analysis of HeLa (left) and HepG2 (right) cells using PTEN mouse mAb (green). Red: Actin filaments have been labeled with DY-554 phalloidin. Blue: DRAQ5 fluorescent DNA dye.

• Flow cytometry

  

  Flow cytometric analysis of HeLa cells using PTEN mouse mAb (right) and negative control (left).

PTEN (phosphatase and tensin homologue deleted on chromosome ten), also referred to as MMAC (mutated in multiple advanced cancers) phosphatase, is a tumor suppressor implicated in a wide variety of human cancers [1]. PTEN encodes a 403 amino acid polypeptide originally described as a dual-specificity protein phosphatase [2]. The main substrates of PTEN are inositol phospholipids generated by the activation of the phosphoinositide 3-kinase (PI3K) [3]. PTEN is a major negative regulator of the PI3K/Akt signaling pathway [1,4,5]. PTEN possesses a carboxy-terminal, noncatalytic regulatory domain with three phosphorylation sites (Ser380, Thr382 and Thr383) that regulate PTEN stability and may affect its biological activity [6,7]. PTEN regulates p53 protein levels and activity [8] and is involved in G protein coupled signaling during chemotaxis [9,10].
References
1. Cantley, L.C. and Neel, B.G. Proc Natl Acad Sci USA 1999; 96: 4240-5.
2. Myers, M.P. et al. Proc Natl Acad Sci USA 1997; 94: 9052-7.
3. Myers, M.P. et al. Proc Natl Acad Sci USA 1998; 95: 13513-8.
4. Wan, X. and Helman, L.J. Oncogene 2003; 22: 8205-11.
5. Wu, X. et al. Proc Natl Acad Sci USA 1998; 95: 15587-91.
6. Vazquez, F. et al. Mol Cell Biol 2000; 20: 5010-8.
7. Torres, J. and Pulido, R. J Biol Chem 2001; 276: 993-8.
8. Freeman, D.J. et al. Cancer Cell 2003; 3: 117-30.
9. Funamoto, S. et al. Cell 2002; 109: 611-23.
10. Iijima, M. and Devreotes, P. Cell 2002; 109: 599-610.