The RNF8 antibody is a crucial tool for studying the role of Ring Finger Protein 8 (RNF8), an E3 ubiquitin ligase involved in DNA damage response (DDR) pathways. RNF8 facilitates repair of DNA double-strand breaks by promoting ubiquitination of histone H2A and recruiting downstream repair proteins like BRCA1 and 53BP1 to damage sites. Its FHA domain interacts with phosphorylated mediators (e.g., MDC1), while the RING domain confers ubiquitin ligase activity. Dysregulation of RNF8 is linked to genomic instability, cancer progression, and chemotherapy resistance.
RNF8 antibodies, typically raised in rabbits or mice, detect endogenous RNF8 via techniques such as Western blotting, immunofluorescence, and immunoprecipitation. They target specific epitopes, often within functional domains, to assess expression levels, subcellular localization, or protein interactions. These antibodies are vital for investigating DDR mechanisms, cellular responses to ionizing radiation, and RNF8's role in maintaining genome integrity. Studies using RNF8-deficient models (e.g., mice with infertility or radiosensitivity) further highlight its biological significance.
As RNF8 emerges as a potential therapeutic target in cancers, its antibodies enable research into small-molecule inhibitors or biomarkers for DDR-related diseases. Validation via knockout controls ensures specificity, underscoring their utility in both basic research and translational applications.