Cell Signaling Technology
XP Monoclonal Antibody

Product Pathways - PI3K / Akt Signaling

PTEN (D4.3) XP® Rabbit mAb (Biotinylated) #4005

Applications Reactivity Sensitivity MW (kDa) Isotype
W IP H M R Hm Mk Endogenous 54 Rabbit IgG

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

Protocols

Specificity / Sensitivity

PTEN (D4.3) XP® Rabbit mAb (Biotinylated) detects endogenous levels of total PTEN protein.

Source / Purification

Monoclonal antibody is produced by immunizing animals with a synthetic peptide corresponding to residues in the carboxy-terminal sequence of human PTEN protein.

Western blot analysis of extracts from various cell lines using PTEN (D4.3) XP® Rabbit mAb (Biotinylated).

Immunoprecipitation of PTEN from HeLa cell lysates using PTEN (D4.3) XP® Rabbit mAb (Biotinylated) and Immobilized Streptavidin (Bead Conjugate) #3419, followed by western blot using PTEN (D4.3) XP® Rabbit mAb #9188 and Mouse Anti-Rabbit IgG (Light-Chain Specific) (L57A3) mAb #3677.

Description

This Cell Signaling Technology (CST) antibody is conjugated to biotin under optimal conditions. The unconjugated PTEN (D4.3) XP® Rabbit mAb #9188 reacts with human, mouse, rat and monkey PTEN protein. PTEN (D4.3) XP® Rabbit mAb (Biotinylated) also recognizes PTEN in these species.

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 levels 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, 4240-5.
  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. Wan, X. and Helman, L.J. (2003) Oncogene 22, 8205-11.
  5. Wu, X. et al. (1998) Proc Natl Acad Sci USA 95, 15587-91.
  6. Vazquez, F. et al. (2000) Mol Cell Biol 20, 5010-8.
  7. Torres, J. and Pulido, R. (2001) J Biol Chem 276, 993-8.
  8. Freeman, D.J. et al. (2003) Cancer Cell 3, 117-30.
  9. Funamoto, S. et al. (2002) Cell 109, 611-23.
  10. Iijima, M. and Devreotes, P. (2002) Cell 109, 599-610.

Application References

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Companion Products

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

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