BARD1 interacts with the N-terminal region of BRCA1. In addition to its ability to bind BRCA1 in vivo and in vitro, BARD1 shares homology with the 2 most conserved regions of BRCA1: the N-terminal RING motif and the C-terminal BRCT domain. The RING motif is a cysteine-rich sequence found in a variety of proteins that regulate cell growth, including the products of tumor suppressor genes and dominant protooncogenes. The BARD1 protein also contains 3 tandem ankyrin repeats. The BARD1/BRCA1 interaction is disrupted by tumorigenic amino acid substitutions in BRCA1, implying that the formation of a stable complex between these proteins may be an essential aspect of BRCA1 tumor suppression. BARD1 may be the target of oncogenic mutations in breast or ovarian cancer.
BARD1 antibody can be used in ELISA, Western Blot, immunohistochemistry starting at 10 μg/mL, immunofluorescence, and immunoprecipitation.
Protein G Column
PBS, 0.1% sodium azide.
Aliquot and store at -20°C or below. Avoid multiple freeze-thaw cycles.