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Product Description

Each control slide contains formalin fixed, paraffin-embedded LNCaP and NIH/3T3 cell pellets. NIH/3T3 cells express PTEN while LNCaP cells do not express PTEN. Western blot analysis was performed on extracts derived from the same cells to verify PTEN expression.

To be used with antibodies: 9188, 9559.


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).


1.  Wan X and Helman LJ (2003) Oncogene 22, 8205–11

2.  Myers, M.P. et al. (1997) Proc Natl Acad Sci USA 94, 9052-7.

3.  Myers, M.P. et al. (1998) Proc Natl Acad Sci USA 95, 13513-8.

4.  Wu, X. et al. (1998) Proc Natl Acad Sci USA 95, 15587-91.

5.  Vazquez, F. et al. (2000) Mol Cell Biol 20, 5010-8.

6.  Torres, J. and Pulido, R. (2001) J Biol Chem 276, 993-8.

7.  Freeman, D.J. et al. (2003) Cancer Cell 3, 117-30.

8.  Funamoto, S. et al. (2002) Cell 109, 611-23.

9.  Cantley, L.C. and Neel, B.G. (1999) Proc Natl Acad Sci USA 96, 4240-5.

10.  Iijima, M. and Devreotes, P. (2002) Cell 109, 599-610.



For Research Use Only. Not For Use In Diagnostic Procedures.
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