Cell Signaling Technology

Product Pathways - Akt Signaling

Non-Phospho PTEN (Ser380/Thr382/Thr383) Antibody #9569

Applications Reactivity MW (kDa) Source
W IP M (H) (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

Non-Phospho PTEN (Ser380/Thr382/Thr383) Antibody detects endogenous levels of PTEN only when dephosphorylated at Ser380, Thr382 and Thr383.

Source / Purification

Polyclonal antibodies are produced by immunizing rabbits with a synthetic peptide (KLH-coupled) corresponding to residues surrounding Ser380/Thr382/Thr383 of human PTEN. Antibodies are purified by peptide affinity chromatography.

Western Blotting

Western Blotting

Western blot analysis of extracts from NIH/3T3 cells, λ phosphatase- or PDGF-treated, using Non-Phospho PTEN (Ser380/Thr382/Thr383) Antibody (upper) or PTEN (138G6) Rabbit mAb #9559 (lower). The non-phospho-specificity of the antibody was verified by preincubating the antibody with no peptide, with PTEN (Ser380/Thr382/Thr383) non-phosphopeptide or with PTEN (Ser380/Thr382/Thr383) phosphopeptide prior to incubating the membrane.

ELISA-Peptide

ELISA-Peptide

Non-Phospho PTEN (Ser380/Thr382/Thr383) Antibody specificity was determined by peptide ELISA. The graphs depict the binding of the various dilutions of the antibody (1:250, 1:500, 1:1000, 0) to pre-coated tri-non-phospho PTEN (Ser380/Thr382/Thr383) peptide, tri-phospho PTEN (Ser380/Thr382/Thr383) peptide, phospho PTEN (Ser380) peptide, phospho PTEN (Thr382) peptide, and phospho PTEN (Thr383) peptide.

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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