Cell Signaling Technology

Product Pathways - Akt Signaling

Phospho-PTEN (Ser380) Antibody #9551

Applications Reactivity MW (kDa) Source
W IP H M R 54 Rabbit

Applications Key:  W=Western Blotting  IP=Immunoprecipitation
Reactivity Key:  H=Human  M=Mouse  R=Rat
Species enclosed in parentheses are predicted to react based on 100% sequence homology. Species cross-reactivity is determined by Western blot.

Specificity / Sensitivity

Phospho-PTEN (Ser380) Antibody detects endogenous levels of PTEN only when phosphorylated at Ser380.

Source / Purification

Polyclonal antibodies are produced by immunizing rabbits with a synthetic phospho-peptide (KLH-coupled) corresponding to residues surrounding Ser380 of human PTEN. Antibodies are purified by protein A and peptide affinity chromatography.

Western Blotting

Western Blotting

Western blot analysis of extracts from various cell lines, using Phospho-PTEN (Ser380) Antibody (upper) or PTEN Antibody #9552 (lower). The phospho-specificity of the antibody was confirmed by treating the membrane with calf intestinal alkaline phosphatase (CIP) after Western transfer.

Background

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 level and activity (8) and is involved in G protein coupled signaling during chemotaxis (9,10).

  1. Cantley, L.C. and Neel, B.G. (1999) Proc. Natl. Acad. Sci. USA 96, 4240-4245.
  2. Myers, M.P. et al. (1997) Proc. Natl. Acad. Sci. USA 94, 9052-9057.
  3. Myers, M.P. et al. (1998) Proc. Natl. Acad. Sci. USA 95, 13513-13518.
  4. Wan, X. and Helman, L.J. (2003) Oncogene 22, 8205-8211.
  5. Wu, X. et al. (1998) Proc. Natl. Acad. Sci. USA 95, 15587-15591.
  6. Vazquez, F. et al. (2000) Mol. Cell. Biol. 20, 5010-5018.
  7. Torres, J. and Pulido, R. (2001) J. Biol. Chem. 276, 993-998.
  8. Freeman, D.J. et al. (2003) Cancer Cell 3, 117-130.
  9. Funamoto, S. et al. (2002) Cell 109, 611-623.
  10. Iijima, M. and Devreotes, P. (2002) Cell 109, 599-610.

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