USP7 (Ubiquitin-Specific Protease 7), also known as HAUSP, is a deubiquitinating enzyme critical for regulating protein stability and function by removing ubiquitin moieties from target proteins. It plays a central role in diverse cellular processes, including DNA repair, epigenetic regulation, immune response, and apoptosis. USP7 is particularly notable for its interaction with tumor suppressors (e.g., p53. PTEN) and oncoproteins (e.g., MDM2. viral proteins), making it a key player in cancer biology, neurodegenerative diseases, and viral pathogenesis.
USP7-specific antibodies are essential tools for studying its expression, localization, and molecular mechanisms. They are widely used in techniques like Western blotting, immunoprecipitation, and immunofluorescence to investigate USP7’s role in substrate recognition, post-translational modifications, and pathway modulation. High-quality USP7 antibodies must exhibit specificity to avoid cross-reactivity with other ubiquitin-specific proteases (e.g., USP5. USP13) due to structural similarities within the USP family. Validation via knockout cell lines or siRNA-mediated depletion is critical to confirm target specificity.
Research on USP7 antibodies has accelerated drug discovery efforts, as USP7 inhibitors are being explored for cancer therapy and antiviral treatments. Reliable antibodies help dissect USP7’s dual roles in promoting or suppressing disease, depending on cellular context, underscoring its therapeutic potential and complexity as a biological target.