Cell Signaling Technology

Product Pathways - Phosphatases

Phospho-PTPα (Tyr789) Antibody #4481

Applications Reactivity Sensitivity MW (kDa) Source
W IP H M R Mk Endogenous 145 Rabbit

Applications Key:  W=Western Blotting  IP=Immunoprecipitation
Reactivity Key:  H=Human  M=Mouse  R=Rat  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

Phospho-PTPα (Tyr789) Antibody detects endogenous levels of PTPα only when phosphorylated at Tyr789. This antibody does not cross-react with other phosphorylated receptor tyrosine phosphatases.

Source / Purification

Polyclonal antibodies are produced by immunizing animals with a synthetic phosphopeptide corresponding to residues surrounding Tyr789 of human PTPα. Antibodies are purified by protein A and peptide affinity chromatography.

Western Blotting

Western Blotting

Western blot analysis of C2C12 and COS cell lysates, untreated or alkaline phosphatase (CIP)-treated, using Phospho-PTPα (Tyr789) Antibody (upper) or PTPα Antibody (Gift from Dr. D. Shalloway, Dept. of Molecular Biology and Genetics, Cornell University, Ithaca, NY.) (lower).

Background

PTPα (PTPRA) is a transmembrane receptor tyrosine phosphatase implicated in the regulation of Src family kinases during the G2 to mitosis entry point. Two identified splice variants differ in the size of the extracellular region; the shorter form appears to be ubiquitously expressed while the larger protein is more limited in distribution (1). The cytoplasmic region of PTPα contains two putative catalytic domains. One phosphatase domain (D1) exhibits catalytic activity while the other (D2) may regulate phosphatase activity by allowing receptor dimer formation (2,3). PTPα is a physiological regulator of Src and Src family kinases (4). Constitutive phosphorylation of the carboxy-terminal Tyr789 of PTPα is essential for dephosphorylation of Src at Tyr527. Phosphorylation of PTPα at this residue also allows binding of the Grb2 inhibitor, restricting PTPα activation of Src (5,6). PKC-mediated phosphorylation of the PTP at Ser180 and Ser204 also increases PTPα phosphatase activity (7).

  1. Kapp, K. et al. (2007) Genes Cells 12, 63-73.
  2. Blanchetot, C. et al. (2002) J Biol Chem 277, 47263-9.
  3. Krueger, N.X. et al. (1990) EMBO J 9, 3241-52.
  4. den Hertog, J. et al. (1993) EMBO J 12, 3789-98.
  5. Zheng, X.M. et al. (2000) EMBO J 19, 964-78.
  6. Zheng, X.M. et al. (2002) J Biol Chem 277, 21922-9.
  7. Tracy, S. et al. (1995) J Biol Chem 270, 10587-94.

Application References

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

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