Phospho-p130 Cas (Tyr410) Antibody

INQUIRY

CAT. NO.: AMA-0549

Target Information
UniProt ID	P56945

Product Details
Size	100 µL
Reactivity	Human, Mouse, Rat
Storage	Store at -20°C. Do not aliquot the antibody.
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.

Usage
Application	WB, IP
Product Usage Information Dilution	Western Blotting (1:1000); Immunoprecipitation (1:50)
MW (Target)	130 kDa

Background
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) and the FAK-related kinase PYK2 as well as the tyrosine phosphatases PTP-1B and PTP-PEST 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 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) 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.

Background

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) and the FAK-related kinase PYK2 as well as the tyrosine phosphatases PTP-1B and PTP-PEST 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 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) 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.

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