BCAR1 Mouse Antibody [Clone ID: M144]

Specifications

Product Data
Clone Name	M144
Applications	ICC, IHC, IP, WB
Recommend Dilution	WB: 1:1000 ICC: 1:200
Reactivity	Human, Rat, Mouse, Chicken
Host	Mouse
Immunogen	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.
Specificity	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.
Formulation	PBS + 1 mg/ml BSA, 0.05% NaN3 and 50% glycerol
Concentration	lot specific
Purification	Protein A Purified
Conjugation	Unconjugated
Storage Condition	Storage at -20°C is recommended, as aliquots may be taken without freeze/thawing due to presence of 50% glycerol. Stable for at least 1 year at -20°C.
Predicted Protein Size	130
Database Link	UniProt ID P56945
Background	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.
Note	Protein G purified tissue culture supernatant.
Reference Data

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