Breast Cancer Anti-Estrogen Resistance 1 (BCAR1) (C-Term) antibody

Details for Product No. ABIN965643
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Antigen
Synonyms MGC68466, cas, Crkas, p130cas, BCAR1, fc17f11, wu:fc17f11, zgc:175192, CAS, CAS1, CASS1, CRKAS, P130Cas, AI385681, Cas, P130CAS
Epitope
C-Term
(30), (18), (17), (17), (12), (5), (4), (3), (3), (3), (2), (2), (2), (1), (1), (1), (1), (1), (1), (1), (1), (1), (1), (1), (1), (1), (1), (1), (1), (1), (1), (1), (1)
Reactivity
Mouse (Murine), Rat (Rattus)
(159), (89), (88), (16), (12), (4), (1), (1)
Host
Rabbit
(143), (21), (2), (2)
Clonality
Polyclonal
Conjugate
Un-conjugated
(8), (5), (5), (5), (5), (5), (5), (5), (5), (5), (5)
Application
Please enquire
(113), (56), (50), (47), (34), (16), (16), (7), (3), (3)
Pubmed 9 references available
Quantity 0.1 mg
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Catalog No. ABIN965643
452.38 $
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Immunogen Polyclonal antibody produced in rabbits immunizing with a synthetic peptide corresponding to C-terminal residues of mouse BCAR1 (Breast cancer anti-estrogen resistance protein 1)
Alternative Name BCAR1
Background BCAR1 (Breast cancer anti-estrogen resistance protein 1) is a docking protein which plays a central coordinating role for tyrosine-kinase-based signaling related to cell adhesion. BCAR1 is implicated in induction of cell migration. Overexpression confers antiestrogen resistance on breast cancer cells. BCAR1 forms complexes in vivo with focal adhesion kinase 1, adapter protein CRKL and LYN kinase. BCAR1 can heterodimerize with CASL. BCAR1 interacts with BCAR3, NPHP1, PTK2B and SH2D3C and interacts with activated CSPG4 as well as interacts with INPPL1/SHIP2. BCAR1 localizes in cell junction, focal adhesion, cytoplasm. The unphosphorylated form localizes in the cytoplasm and can move to the membrane upon tyrosine phosphorylation. BCAR1 is 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. BCAR1 contains a central domain (substrate domain) containing multiple potential SH2-binding sites and a C-terminal domain containing a divergent helix-loop-helix (HLH) motif. The SH2-binding sites putatively bind CRK, NCK and ABL SH2 domains. The HLH motif is absolutely required for the induction of pseudohyphal growth in yeast and mediates heterodimerization with CASL. A serine-rich region promotes activation of the serum response element (SRE). The SH3 domain is necessary for the localization of the protein to focal adhesions and interacts with one proline-rich region of focal adhesion kinase 1. Focal adhesion kinase 1 phosphorylates the protein at the YDYVHL motif. SRC-family kinases are recruited to the phosphorylated sites and can phosphorylate other tyrosine residues. Tyrosine phosphorylation is triggered by integrin mediated adhesion of cells to the extracellular matrix.
Synonyms: CAS, CASS1 (Cas scaffolding protein family member 1), CRKAS (CRK-associated substrate, p130cas),
Research Area Cancer, Tyrosine Kinases
Restrictions For Research Use only
Product cited in: Brinkman, van der Flier, Kok et al.: "BCAR1, a human homologue of the adapter protein p130Cas, and antiestrogen resistance in breast cancer cells." in: Journal of the National Cancer Institute, Vol. 92, Issue 2, pp. 112-20, 2000 (PubMed).

Prasad, Topping, Decker: "SH2-containing inositol 5'-phosphatase SHIP2 associates with the p130(Cas) adapter protein and regulates cellular adhesion and spreading." in: Molecular and cellular biology, Vol. 21, Issue 4, pp. 1416-28, 2001 (PubMed).

Rush, Moritz, Lee et al.: "Immunoaffinity profiling of tyrosine phosphorylation in cancer cells." in: Nature biotechnology, Vol. 23, Issue 1, pp. 94-101, 2005 (PubMed).

Zhang, Wolf-Yadlin, Ross et al.: "Time-resolved mass spectrometry of tyrosine phosphorylation sites in the epidermal growth factor receptor signaling network reveals dynamic modules." in: Molecular & cellular proteomics : MCP, Vol. 4, Issue 9, pp. 1240-50, 2005 (PubMed).

Sjöblom, Jones, Wood et al.: "The consensus coding sequences of human breast and colorectal cancers. ..." in: Science (New York, N.Y.), Vol. 314, Issue 5797, pp. 268-74, 2006 (PubMed).

Beausoleil, Villén, Gerber et al.: "A probability-based approach for high-throughput protein phosphorylation analysis and site localization." in: Nature biotechnology, Vol. 24, Issue 10, pp. 1285-92, 2006 (PubMed).

Olsen, Blagoev, Gnad et al.: "Global, in vivo, and site-specific phosphorylation dynamics in signaling networks." in: Cell, Vol. 127, Issue 3, pp. 635-48, 2006 (PubMed).

Rikova, Guo, Zeng et al.: "Global survey of phosphotyrosine signaling identifies oncogenic kinases in lung cancer. ..." in: Cell, Vol. 131, Issue 6, pp. 1190-203, 2007 (PubMed).

Dephoure, Zhou, Villén et al.: "A quantitative atlas of mitotic phosphorylation." in: Proceedings of the National Academy of Sciences of the United States of America, Vol. 105, Issue 31, pp. 10762-7, 2008 (PubMed).

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