PSME1 (Proteasome Activator Subunit 1), also known as PA28α, is a key component of the 11S regulatory complex (PA28) that activates the 20S proteasome, a critical protease responsible for degrading ubiquitinated proteins. This subunit plays a vital role in the ubiquitin-proteasome system, which regulates protein turnover, cellular homeostasis, and antigen processing for major histocompatibility complex (MHC) class I presentation. PSME1 forms a heteroheptameric complex with PSME2 (PA28β) or homooligomers, enhancing proteasomal cleavage activity and generating antigenic peptides for immune recognition.
PSME1 antibodies are widely used in research to study proteasome function, immune responses, and diseases linked to proteasomal dysregulation, such as cancer, autoimmune disorders, and neurodegenerative conditions. Elevated PSME1 expression has been observed in various cancers, correlating with tumor progression, drug resistance, and immune evasion. Its involvement in antigen processing also makes it a focus in immunotherapy and vaccine development.
Commercially available PSME1 antibodies are typically developed using recombinant protein fragments or synthetic peptides as immunogens. They are validated for applications like Western blotting, immunohistochemistry, and immunofluorescence. Researchers rely on these antibodies to explore PSME1's regulatory mechanisms, interactions with other proteasome subunits, and potential as a therapeutic target. However, specificity and cross-reactivity with homologous subunits (e.g., PSME2) require careful validation in experimental settings.