phospho-p130 Cas (Tyr-751) Peptide peptide product blog
Tags: Peptide; phospho-p130 Cas (Tyr-751) Peptide; phospho-p130 Cas (Tyr-751) Peptide peptide;
The phospho-p130 Cas (Tyr-751) Peptide n/a (Catalog #MBS474046) is a Peptide and is intended for research purposes only. The product is available for immediate purchase.Antibody Blocking: 1 ug/ml
ELISA: 10-100 ng/well. Researchers should empirically determine the suitability of the phospho-p130 Cas (Tyr-751) Peptide n/a for an application not listed in the data sheet. Researchers commonly develop new applications and it is an integral, important part of the investigative research process. The amino acid sequence is listed below:
Peptide Sequence: Phospho-p1 30 Cas (Tyr-751) synthetic peptide correspond s to amino acid residues around tyrosine 751 in rat p130 Cas. This rat sequence is the same as Tyr-653 in human p130 Cas and Tyr-653 in mouse p130 Cas. This site is not conserved in other Cas family members.
To buy or view more detailed product information and pricing, please click on the technical datasheet page below:
p130 Cas (Crk-associated substrate (CAS), breast cancer antiestrogen resistance 1 (BCAR1)) 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) and the FAK-related kinase PYK2, as well as with the tyrosine phosphatases PTP-1B and PTP-PEST. The carboxy-terminal Src binding domain (SBD) contains a prolinerich motif that mediates interaction with the SH3 domains of Src-family kinases (SFKs) and a tyrosine phosphorylation site (Tyr-762 in rat or Tyr-668 in mouse p130 Cas) that can promote interaction with the SH2 domain of SFKs. The p130 Cas central substrate domain, the major region of tyrosine phosphorylation, is characterized by 15 tyrosines present in Tyr-X-Xpro (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, including the adaptors Crk and Nck. In addition, phosphorylation of Tyr- 751 (Tyr-657 in human) near the C-terminal caspase recognition site can attenuate caspase cleavage. Dephosphorylation of this site occurs during apoptosis, and may facilitate p130 Cas degradation.