BCAR3 Antibody
- SPECIFICATION
- CITATIONS
- PROTOCOLS
- BACKGROUND
Application
| WB, IF, E |
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Primary Accession | O75815 |
Other Accession | NP_003558, 4502371 |
Reactivity | Human, Mouse, Rat |
Host | Rabbit |
Clonality | Polyclonal |
Isotype | IgG |
Calculated MW | 91 kDa |
Application Notes | BCAR3 antibody can be used for detection of BCAR3 by Western blot at 1 - 2 µg/mL. For immunofluorescence start at 20 µg/mL. |
Gene ID | 8412 |
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Target/Specificity | BCAR3; At least four isoforms of BCAR3 are known to exist; this antibody will only recognize the largest isoform. BCAR3 antibody is predicted to not cross-react with other BCAR proteins. |
Reconstitution & Storage | BCAR3 antibody can be stored at 4℃ for three months and -20℃, stable for up to one year. As with all antibodies care should be taken to avoid repeated freeze thaw cycles. Antibodies should not be exposed to prolonged high temperatures. |
Precautions | BCAR3 Antibody is for research use only and not for use in diagnostic or therapeutic procedures. |
Name | BCAR3 |
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Synonyms | NSP2, SH2D3B |
Function | Acts as an adapter protein downstream of several growth factor receptors to promote cell proliferation, migration, and redistribution of actin fibers (PubMed:24216110). Specifically involved in INS/insulin signaling pathway by mediating MAPK1/ERK2-MAPK3/ERK1 activation and DNA synthesis (PubMed:24216110). Promotes insulin- mediated membrane ruffling (By similarity). In response to vasoconstrictor peptide EDN1, involved in the activation of RAP1 downstream of PTK2B via interaction with phosphorylated BCAR1 (PubMed:19086031). Inhibits cell migration and invasion via regulation of TGFB-mediated matrix digestion, actin filament rearrangement, and inhibition of invadopodia activity (By similarity). May inhibit TGFB- SMAD signaling, via facilitating BCAR1 and SMAD2 and/or SMAD3 interaction (By similarity). Regulates EGF-induced DNA synthesis (PubMed:18722344). Required for the maintenance of ocular lens morphology and structural integrity, potentially via regulation of focal adhesion complex signaling (By similarity). Acts upstream of PTPRA to regulate the localization of BCAR1 and PTPRA to focal adhesions, via regulation of SRC-mediated phosphorylation of PTPRA (By similarity). Positively regulates integrin-induced tyrosine phosphorylation of BCAR1 (By similarity). Acts as a guanine nucleotide exchange factor (GEF) for small GTPases RALA, RAP1A and RRAS (By similarity). However, in a contrasting study, lacks GEF activity towards RAP1 (PubMed:22081014). |
Cellular Location | Cytoplasm {ECO:0000250|UniProtKB:Q9QZK2}. Cell junction, focal adhesion {ECO:0000250|UniProtKB:Q9QZK2} Note=Localization to focal adhesions depends on interaction with PTPRA {ECO:0000250|UniProtKB:Q9QZK2} |
Tissue Location | Ubiquitously expressed. Found in several cancer cell lines, but not in nonmalignant breast tissue |
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Provided below are standard protocols that you may find useful for product applications.
Background
BCAR3 Antibody: Breast cancer anti-estrogen resistance 3 (BCAR3) was identified in the search for genes involved in the development of estrogen resistance. It contains a putative src homology 2 (SH2) domain and is partly homologous to the cell division cycle protein CDC48. BCAR3 is a binding partner with Cas, an adapter molecule that plays a role in cell proliferation, survival, cell adhesion, and mobility. BCAR3 functions synergistically with Cas to enhance Src activation and promote cell migration, and has been suggested to regulate Cas/Src association, Src kinase activity, and breast cancer adhesion signaling.
References
van Agthoven T, van Agthoven TL, Dekker A, et al. Identification of BCAR3 by a random search for genes involved in antiestrogen resistnace of human breast cancer cells. EMBO J. 1998; 17:2799-808.
Riggins RB, Quilliam LA, and Bouton AH. Synergistic promotion of c-Src activation and cell migration by Cas and AND-34/BCAR3. J. Biol. Chem. 2003; 278:28264-73.
Schuh NR, Guerrero MS, Schrecengost RS, et al. BCAR3 regulates Src/p130Cas association, Src kinase activity, and breast cancer adhesion signaling. J. Biol. Chem. 2010; 285:2309-17.
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