Anti-p130 Cas (C-terminal region) Antibody

P130 Cas (Crk-associated substrate (CAS), breast cancer antiestrogen resistance 1 (BCAR1) ) is a docking protein containing multiple protein-protein interaction domains. The N-terminal SH3 domain functions as a molecular switch regulating CAS tyrosine phosphorylation, as it interacts with tyrosine kinases and phosphatases. The C-terminal Src binding domain contains a proline-rich motif that mediates interaction with the SH3 domains of Src-family kinases (SFKs) . Phosphorylation of this domain at Tyr-762 in rat (Tyr-668 in mouse) promotes this interaction. The p130 Cas central substrate domain is characterized by 15 tyrosines present in Tyr-X-X-Pro (YXXP) motifs, including Tyr-165, Tyr-249, and Tyr-410. When phosphorylated, most YXXP motifs are able to serve as docking sites for proteins with SH2 or PTB domains. In addition, phosphorylation of Tyr-751 (Tyr-653 in human) near the C-terminal caspase recognition site can attenuate caspase cleavage, while dephosphorylation occurs during apoptosis and may facilitate p130 Cas degradation.

Our p130 Cas (C-terminal region) primary antibody from PhosphoSolutions is mouse monoclonal. It detects chicken, human, mouse, and rat p130 Cas (C-terminal region) and is Protein A purified. It is great for use in WB, ICC, IHC, IP.

Clone M144 was generated from a recombinant protein containing amino acid residues in the C-terminal region of rat p130 Cas. This rat sequence is highly conserved in human, mouse, and chicken p130 Cas.

For research use only. Not intended for therapeutic or diagnostic use. Use of all products is subject to our terms and conditions, which can be viewed on our website.

The antibody detects a 130 kDa* protein corresponding to the molecular mass of p130 Cas on SDS-PAGE immunoblots of human A431, endothelial, and Hct116 cells.