Cell Signaling Technology

Product Pathways - Phosphatases

PTP-PEST (AG10) Mouse mAb #4864

Applications Reactivity MW (kDa) Source Isotype
W IP H M R Mk 110 to 125 Mouse IgG1

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

Specificity / Sensitivity

PTP-PEST (AG10) Mouse mAb detects endogenous levels of total PTP-PEST protein. This antibody does not cross-react with other protein tyrosine phosphatases.

Source / Purification

Monoclonal antibody is produced by immunizing mice with human PTP-PEST recombinant protein. The antibody recognizes an epitope within the amino-terminal 305 residues.

Western Blotting

Western Blotting

Western blot analysis of extracts from THP1, HeLa and U-937 cells, using PEP-PEST (AG10) Mouse mAb.

Background

PTP-PEST is a ubiquitously expressed cytosolic protein tyrosine phosphatase with multiple proline-rich regions that appear to be the the docking sites for PTP-PEST binding partners or substrates (1). PTP-PEST regulates fibroblast adhesion, migration and cytokinesis through its association with and dephosphorylation of p130 Cas, paxillin, PSTPIP1, WASp, and other adhesion molecules (1-5). By modulating phosphorylation states of Shc, Pyk2, Fak and WASp, PTP-PEST negatively regulates of lymphocyte activation (1,6). In mammary epithelial cells, EGF facilitates the dephosphorylation of Jak2 by PTP-PEST, thereby interfering with lactogenic hormone PRL signaling (7). PTP-PEST dephosphorylates c-Abl as well, which affects the phosphorylation states of PTP-PEST substates such as paxillin, p130 Cas, Crk and PSTPIP1 (8).

  1. Davidson, D. and Veillette, A. (2001) EMBO J. 20, 3414-3426.
  2. Garton, A.J. and Tonks, N.K. (1999) J. Biol. Chem. 274, 3811-3818.
  3. Shen, Y. et al. (2000) J. Biol. Chem. 275, 1405-1413.
  4. Angers-Loustau, A. et al. (1999) J. Cell Biol. 144, 1019-1031.
  5. Cote, J. et al. (2002) J. Biol. Chem. 277, 2973-2986.
  6. Badour, K. et al. (2003) J. Exp. Med. 199, 99-111.
  7. Horsch, K. et al. (2001) Mol. Endocrinol. 15, 2182-2196.
  8. Cong, F. et al. (2000) Mol. Cell 6, 1413-1423.

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