Catalog # PM1441
p130 Cas (C-terminal region)
Size 100 μl
Species Reactivity Hu, Rt, Ms, Ck
MW 130 kDa
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.
Shin, N-Y. et al. (2004). J Biol Chem. 279(37):38331.
Kim, D.H. et al. (2003). Biochem Biophys Res Comm. 300:141.
Pellicena, P. & Miller, W.T. (2001) J Biol Chem. 276 (30):28190.
Nakamoto, T. et al. (1996) J Biol Chem. 271(15):8959.
*For more information, see UniProt Accession Q63767
The products are are safely shipped at ambient temperature for both domestic and international shipments. Each product is guaranteed to match the specifications as indicated on the corresponding technical data sheet. Please store at -20C upon arrival for long term storage.
*All molecular weights (MW) are confirmed by comparison to Bio-Rad Rainbow Markers and to western blot mobilities of known proteins with similar MW.
Product References:Wilke, G.A. & Wardenburg, J.B. (2010) PNAS. 107(30):13473. (WB: human A459)
This kit contains: