SIRT7 is a member of the sirtuin family of NAD⁺-dependent protein deacetylases, which play roles in chromatin modification, genome stability, and metabolic regulation. Specifically, SIRT7 is localized to the nucleolus and is highly expressed in metabolically active tissues such as the liver and heart. It is implicated in regulating ribosomal DNA (rDNA) transcription, DNA damage repair, and cellular stress responses. SIRT7’s enzymatic activity has been linked to aging, cancer, and metabolic disorders, with studies showing its overexpression in certain cancers (e.g., breast, liver) and its role in promoting tumorigenesis through epigenetic modulation.
SIRT7 antibodies are essential tools for investigating its expression, localization, and function. These antibodies are typically generated using immunogenic peptides or recombinant SIRT7 protein fragments as antigens, often in hosts like rabbits or mice. Validated antibodies enable applications such as Western blotting, immunofluorescence, immunohistochemistry, and co-immunoprecipitation. However, specificity remains a critical consideration due to potential cross-reactivity with other sirtuin family members (e.g., SIRT1 or SIRT6). Researchers frequently validate SIRT7 antibodies using knockout cell lines or siRNA-mediated knockdown to confirm target specificity. Commercial antibodies often provide data on species reactivity, post-translational modification detection, and recommended experimental conditions. Recent studies employing SIRT7 antibodies have clarified its role in nucleolar stress responses, lipid metabolism, and interactions with non-coding RNAs, underscoring its therapeutic potential in age-related diseases and cancer.