The PSMD3 (Proteasome 26S Subunit, Non-ATPase 3) antibody is a tool used to study the PSMD3 protein, a key component of the 26S proteasome. The 26S proteasome is a multi-subunit complex responsible for ubiquitin-dependent protein degradation, playing a critical role in maintaining cellular homeostasis by regulating protein turnover, cell cycle progression, apoptosis, and stress responses. PSMD3. also known as Rpn3. is part of the 19S regulatory particle (RP) that recognizes ubiquitinated proteins, removes ubiquitin tags, and unfolds substrates for translocation into the proteolytic 20S core.
PSMD3 contains a PCI (Proteasome-COP9-eIF3) domain, which facilitates interactions within the 19S RP and other protein complexes. Its expression is linked to various cellular processes, including DNA repair and signal transduction. Dysregulation of proteasome activity, including PSMD3 function, has been implicated in cancer, neurodegenerative diseases, and autoimmune disorders. For example, elevated PSMD3 levels are observed in certain cancers, correlating with poor prognosis and drug resistance.
Antibodies targeting PSMD3 are essential for investigating its expression, localization, and molecular interactions via techniques like Western blotting, immunohistochemistry, and immunoprecipitation. They also aid in exploring the therapeutic potential of proteasome inhibition in diseases. Research using PSMD3 antibodies contributes to understanding proteasome biology and developing targeted therapies, particularly in oncology.