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-AAE knock-in mice express three amino acid substitutions: F125A (phenylalanine to alanine), aspartic acid to alanine D127A (aspartic acid to alanine), and A128E, (alanine to glutamic acid). The mutations correspond to human mutations (F133, D135, F136) described by Zhao et al. (Nature 550: 360-365, 2017) that disrupt the interaction of BARD1 with Rad51 and impair 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-AAE knock-in mice express F125A, D127A, A128E amino acid substitutions 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.