The PSMD4 antibody targets the 26S proteasome regulatory subunit 4 (PSMD4), also known as S5a or Rpn10. a critical component of the 19S regulatory particle within the ubiquitin-proteasome system (UPS). PSMD4 plays a pivotal role in recognizing and binding polyubiquitinated substrates, facilitating their recruitment to the proteasome for degradation. This process is essential for maintaining cellular protein homeostasis, regulating cell cycle progression, and modulating stress responses. Dysregulation of PSMD4 has been implicated in various pathologies, including cancer, neurodegenerative diseases, and autoimmune disorders, making it a key focus in proteostasis-related research.
PSMD4 antibodies are widely used in molecular and cellular studies to investigate proteasome dynamics, substrate recognition mechanisms, and UPS dysfunction. These antibodies enable the detection and quantification of PSMD4 expression in tissues or cell lysates via techniques like Western blotting, immunohistochemistry, and immunofluorescence. Additionally, they are employed in co-immunoprecipitation assays to explore protein-protein interactions within the proteasome complex. Researchers often utilize PSMD4 antibodies to study disease models, screen therapeutic agents targeting the UPS, or validate proteasome activity under stress conditions. Both monoclonal and polyclonal variants are available, with specificity validated across species, including human, mouse, and rat. Understanding PSMD4's role through antibody-based approaches continues to advance insights into proteasome biology and its therapeutic potential.