Cell Signaling Technology

Product Pathways - Tyrosine Kinase / Adaptors

Phospho-p130 Cas (Tyr165) Antibody #4015

Applications Reactivity Sensitivity MW (kDa) Source
W H M R Endogenous 130 Rabbit

Applications Key:  W=Western Blotting
Reactivity Key:  H=Human  M=Mouse  R=Rat
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-p130 Cas (Tyr165) Antibody detects endogenous levels of p130 Cas only when phosphorylated at tyrosine 165. The antibody may cross-react with other phosphorylated tyrosines in the substrate domain of p130 Cas. The antibody may cross-react with phosphorylated PDGFR.

Source / Purification

Polyclonal antibodies are produced by immunizing animals with a synthetic phosphopeptide corresponding to residues surrounding Tyr165 of human p130 Cas. Antibodies are purified by proteinA and peptide affinity chromatography.

Western Blotting

Western Blotting

Western blot analysis of extracts from NIH-3T3 cells, untreated or calf intestinal phosphotase (CIP)-treated, using Phospho-p130 Cas (Tyr165) Antibody (upper) or p130 Cas antibody (lower).

Background

p130 Cas (Crk-associated substrate) is a docking protein containing multiple protein-protein interaction domains. The amino-terminal SH3 domain may function as a molecular switch regulating CAS tyrosine phosphorylation, as it interacts with focal adhesion kinase (FAK) (1) and the FAK-related kinase PYK2 (2), as well as the tyrosine phosphatases PTP-1B (3) and PTP-PEST (4). The carboxy-terminal Src binding domain (SBD) contains a proline-rich motif that mediates interaction with the SH3 domains of Src-family kinases (SFKs) and a tyrosine phosphorylation site (Tyr668 and/or Tyr670) that can promote interaction with the SH2 domain of SFKs (5). The p130 Cas central substrate domain, the major region of tyrosine phosphorylation, is characterized by 15 tyrosines present in Tyr-X-X-Pro (YXXP) motifs, including Tyr165, 249, and 410. When phosphorylated, most YXXP motifs are able to serve as docking sites for proteins with SH2 or PTB domains including adaptors, C-Crk, Nck, and inositol 5'-phosphatase 2 (SHIP2) (6). The tyrosine phosphorylation of p130 Cas has been implicated as a key signaling step in integrin control of normal cellular behaviors including motility, proliferation, and survival. Aberrant Cas tyrosine phosphorylation may contribute to cell transformation by certain oncoproteins (5).

  1. Polte, T.R. and Hanks, S.K. (1997) J Biol Chem 272, 5501-9.
  2. Astier, A. et al. (1997) J. Biol. Chem. 272, 228-232.
  3. Liu, F. et al. (1996) J. Biol. Chem. 271, 31290-31295.
  4. Garton, A. J. et al. (1997) Oncogene 15, 877-885.
  5. Ruest, P.J. et al. (2001) Mol Cell Biol 21, 7641-52.
  6. Bouton, A. H. et al. (2001) Oncogene 20, 6448-6458.

Application References

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

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