The RAD51 antibody is a crucial tool in studying the molecular mechanisms of DNA repair and genome stability. RAD51. a highly conserved protein, plays a central role in homologous recombination repair (HRR) by facilitating strand exchange between damaged DNA and intact homologous sequences. This process is vital for repairing double-strand breaks (DSBs), which, if unrepaired, can lead to genomic instability, carcinogenesis, or cell death. RAD51 forms nucleoprotein filaments on single-stranded DNA, enabling homology search and recombination. Its activity is tightly regulated and often dysregulated in cancers, particularly those with BRCA1/2 mutations (e.g., breast and ovarian cancers), making it a biomarker of "BRCAness" and a predictor of PARP inhibitor sensitivity.
RAD51 antibodies are widely used in research to detect RAD51 expression, localization, and foci formation (indicative of active HRR) through techniques like immunofluorescence, Western blotting, and immunohistochemistry. These antibodies help assess HRR proficiency in cancer cells, study synthetic lethality in BRCA-deficient tumors, and investigate chemoresistance mechanisms. Commercially available RAD51 antibodies are typically raised against conserved epitopes, often validated for cross-reactivity in human, mouse, and rat models. Quality validation includes testing in knockout cell lines to confirm specificity. Recent applications also extend to developmental biology and understanding replication stress responses. Proper antibody selection depends on the experimental model and detection method, emphasizing the need for rigorous validation to ensure accurate interpretation of RAD51's dynamic roles in genome maintenance.