|Calculated MW||93372 Da|
|Other Names||Breast cancer anti-estrogen resistance protein 1, CRK-associated substrate, Cas scaffolding protein family member 1, p130cas, BCAR1, CAS, CASS1, CRKAS|
|Target/Specificity||A synthetic peptide corresponding to residues surrounding Tyrosine 410 of human p130Cas was used as an immunogen.|
|Format||50 mM Tris-Glycine (pH 7.4), 0.15 M NaCl, 40% Glycerol, 0.01% sodium azide and 0.05% BSA.|
|Storage||Maintain refrigerated at 2-8°C for up to 6 months. For long term storage store at -20°C in small aliquots to prevent freeze-thaw cycles.|
|Precautions||p130Cas Antibody Phospho (pY410) is for research use only and not for use in diagnostic or therapeutic procedures.|
|Synonyms||CAS, CASS1, CRKAS|
|Function||Docking protein which plays a central coordinating role for tyrosine kinase-based signaling related to cell adhesion. Implicated in induction of cell migration. Overexpression confers antiestrogen resistance on breast cancer cells.|
|Cellular Location||Cell junction, focal adhesion. Cytoplasm. Note=Unphosphorylated form localizes in the cytoplasm and can move to the membrane upon tyrosine phosphorylation.|
|Tissue Location||Widely expressed with an abundant expression in the testis. Low level of expression seen in the liver, thymus, and peripheral blood leukocytes. The protein has been detected in a B-cell line|
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Provided below are standard protocols that you may find useful for product applications.
Breast cancer anti-estrogen resistance protein 1 (p130Cas) is a docking protein that plays a central coordinating role for tyrosine kinase-based signaling related to cell adhesion (1). It has defined function in cardiovascular development, actin filament assembly and Src-induced transformation (2). p130Cas is highly phosphorylated at tyrosines during transformation by v-Src, as well as by v-Crk, forming stable complexes with these oncoproteins. Cytoplasmic p130Cas has been shown to move to the membrane upon tyrosine phosphorylation. p130Cas is a common cellular target of phosphorylation signal via v-Crk and v-Src oncoproteins, and its unique structure indicates its possible role in assembling signals from multiple SH2-containing molecules (3). It is implicated in induction of cell migration, and over expression of p130Cas confers anti-estrogen resistance on breast cancer cells (1).
1. The UniProt Consortium. The Universal Protein Resource (UniProt), Nucleic Acids Res. 36:D190-D195 (2008). 2. Ruest PJ., et al. Mol Cell Biol. 21(22):7641-52, 2001 3. Bouton AH., et al. Oncogene 20(44):6448-58, 2001
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