Product Pathways - Tyrosine Kinase / Adaptors
Phospho-p130 Cas (Tyr410) Antibody #4011
|W IP||H M R||Endogenous||130||Rabbit|
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.
Specificity / Sensitivity
Phospho-p130 Cas (Tyr410) Antibody detects endogenous levels of p130 Cas only when phosphorylated at tyrosine 410. The antibody may cross-react with other phosphorylated tyrosines in the substrate domain of p130 Cas and paxillin. 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 Tyr410 of human p130 Cas. Antibodies are purified by proteinA and peptide affinity chromatography.
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).
- Polte, T.R. and Hanks, S.K. (1997) J Biol Chem 272, 5501-9.
- Astier, A. et al. (1997) J. Biol. Chem. 272, 228-232.
- Liu, F. et al. (1996) J. Biol. Chem. 271, 31290-31295.
- Garton, A. J. et al. (1997) Oncogene 15, 877-885.
- Ruest, P.J. et al. (2001) Mol Cell Biol 21, 7641-52.
- Bouton, A. H. et al. (2001) Oncogene 20, 6448-6458.
- Fonseca, P. M. et al. (2004) Regulation and localization of CAS substrate domain tyrosine phosphorylation. Cellular Signalling 16 (5), 621-629. Applications: IC-IF Western Blotting
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For Research Use Only. Not For Use In Diagnostic Procedures.