The PSMD14 antibody is a crucial tool for studying the 26S proteasome regulatory subunit, a component of the ubiquitin-proteasome system responsible for targeted protein degradation. PSMD14 (Proteasome 26S Subunit, Non-ATPase 14), also known as POH1 or RPN11. is part of the 19S regulatory particle that recognizes and deubiquitinates polyubiquitinated substrates, enabling their translocation into the proteolytic 20S core. This subunit contains a conserved JAMM/MPN domain critical for its metalloisopeptidase activity, distinguishing it from other regulatory particles.
Researchers use PSMD14 antibodies in techniques like Western blotting, immunoprecipitation, and immunofluorescence to investigate proteasome assembly, protein turnover mechanisms, and cellular responses to proteasome inhibitors (e.g., bortezomib). Its expression and function are implicated in cancer progression, neurodegenerative diseases (e.g., Alzheimer’s), and immune regulation, making it a potential therapeutic target. Commercially available antibodies are typically validated for specificity in human, mouse, or rat samples, with some targeting epitopes in the N-terminal or JAMM domains. Studies employing these antibodies have clarified PSMD14’s role in maintaining genomic stability, cell cycle control, and apoptosis. However, users should verify cross-reactivity and optimal experimental conditions due to structural similarities with other proteasomal subunits.