Bard1 (BRCA1 associated RING domain 1) encodes a protein that interacts with the N-terminal region of BRCA1 and has homology with the 2 most conserved regions of BRCA1, the N-terminal RING motif and the C-terminal BRCT domain. The BARD1/BRCA1 interaction is implicated in tumor suppression. Mutations in BARD1 are associated with breast cancer and hereditary breast ovarian cancer syndrome. Bard1-K132N knock-in mice express a codon 132&nbsp; lysine to asparagine amino acid substitution (K132N). The mutation corresponds to the human tumor-associated mutation, K140N, described by Zhao et al. (Nature 550: 360-365, 2017) and found in two patients with colorectal carcinoma or uterine corpus endometrial carcinoma. The conserved residue K140 is located next to the FXDA motif. The alteration disrupts the interaction of BARD1 with RAD51 and impairs the strand-invasion step of homologous recombination. Mice homozygous for the mutations are viable and fertile. This strain may be useful in studies of tumor suppression and breast cancer.

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Bard1-K132N knock-in mice express the codon 132 amino acid substitution&nbsp;lysine to asparagine in the Bard1 (BRCA1 associated RING domain 1) locus. This strain may be useful in studies of tumor suppression and breast cancer.

This strain is hosted by NIH's MMRRC, which partners with JAX for the distribution of this and other strains. For additional information and to purchase, please visit the MMRRC site.