• Product nameAnti-BCAR1 antibody
    See all BCAR1 primary antibodies
  • Description
    Rabbit polyclonal to BCAR1
  • SpecificityThis antibody detects endogenous levels of total BCAR1 protein.
  • Tested applicationsSuitable for: ELISA, IHC-Pmore details
  • Species reactivity
    Reacts with: Mouse, Rat, Human
  • Immunogen

    Synthetic non-phosphopeptide designed around the phosphorylation site of tyrosine 410, of human BCAR1.

  • Positive control
    • Human breast carcinoma tissue (IHC-P).


  • FormLiquid
  • Storage instructionsShipped at 4°C. Upon delivery aliquot and store at -20°C. Avoid freeze / thaw cycles.
  • Storage bufferPreservative: 0.02% Sodium Azide
    Constituents: 50% Glycerol, PBS (without Mg2+ and Ca2+), 150mM Sodium chloride, pH 7.4
  • Concentration information loading...
  • PurityImmunogen affinity purified
  • Purification notesThe antibody was affinity-purified from rabbit antiserum by affinity-chromatography using epitope-specific immunogen.
  • ClonalityPolyclonal
  • IsotypeIgG
  • Research areas


Our Abpromise guarantee covers the use of ab52198 in the following tested applications.

The application notes include recommended starting dilutions; optimal dilutions/concentrations should be determined by the end user.

Application Abreviews Notes
ELISA 1/10000.
IHC-P Use at an assay dependent concentration.


  • FunctionDocking 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.
  • Tissue specificityWidely 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.
  • Sequence similaritiesBelongs to the CAS family.
    Contains 1 SH3 domain.
  • DomainContains 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 ABL1 SH2 domains. The HLH motif is absolutely required for the induction of pseudohyphal growth in yeast and mediates heterodimerization with NEDD9.
    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 PTK2/FAK11.
  • Post-translational
    PTK2/FAK1 activation mediates phosphorylation at the YDYVHL motif; phosphorylation is most likely catalyzed by SRC family members. 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.
    Dephosphorylated by PTPN14 at Tyr-128.
  • Cellular localizationCell junction, focal adhesion. Cytoplasm. Unphosphorylated form localizes in the cytoplasm and can move to the membrane upon tyrosine phosphorylation.
  • Information by UniProt
  • Database links
  • Alternative names
    • BCAR 1 antibody
    • Bcar1 antibody
    • BCAR1_HUMAN antibody
    • Breast cancer anti estrogen resistance 1 antibody
    • Breast cancer anti estrogen resistance 1 protein antibody
    • Breast cancer anti-estrogen resistance protein 1 antibody
    • CAS antibody
    • Cas scaffolding protein family member 1 antibody
    • CAS1 antibody
    • Cass1 antibody
    • Crk associated substrate antibody
    • Crk associated substrate p130Cas antibody
    • CRK-associated substrate antibody
    • CRKAS antibody
    • FLJ12176 antibody
    • FLJ45059 antibody
    • p130cas antibody
    see all

Anti-BCAR1 antibody images

  • Paraffin-embedded human breast carcinoma tissue stained for BCAR1, using ab52198 (1/50). The right-hand panel represents a negative control where ab52198 was pre-incubated with the immunizing (blocking) peptide.

References for Anti-BCAR1 antibody (ab52198)

This product has been referenced in:
  • Levental KR  et al. Matrix crosslinking forces tumor progression by enhancing integrin signaling. Cell 139:891-906 (2009). ICC/IF ; Human . Read more (PubMed: 19931152) »

See 1 Publication for this product

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