BRD3 (Bromodomain-containing protein 3) is a member of the BET (bromodomain and extraterminal) protein family, which plays a key role in epigenetic regulation by recognizing acetylated lysine residues on histones and other proteins. As an epigenetic "reader," BRD3 binds to acetylated chromatin via its two bromodomains, facilitating transcriptional activation or repression of genes involved in cell proliferation, inflammation, and oncogenesis. Its dysregulation has been linked to cancers, inflammatory diseases, and viral infections.
BRD3 antibodies are essential tools for studying its function, localization, and interactions in both normal and pathological contexts. These antibodies are widely used in techniques like Western blotting, immunofluorescence, chromatin immunoprecipitation (ChIP), and co-immunoprecipitation (Co-IP) to detect BRD3 expression, map chromatin-binding sites, or identify protein complexes. High-quality BRD3 antibodies exhibit specificity for unique epitopes, distinguishing BRD3 from closely related BET family members like BRD2 and BRD4. Validation across applications and species (e.g., human, mouse) is critical to ensure reliability.
Research on BRD3 has gained momentum due to the therapeutic potential of BET inhibitors in cancer and inflammatory disorders. BRD3-specific antibodies help dissect its distinct biological roles, assess inhibitor efficacy, and explore compensatory mechanisms in drug resistance. However, cross-reactivity and batch variability remain challenges, emphasizing the need for rigorous antibody validation in experimental systems.