PSMA1抗体

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     Gel: 12%SDS-PAGE, Lysate: 40 μg, Lane 1-7: SKOV3, 293T, Raji, PC-3, HepG2, Hela and Jurkat cell lysates, Primary antibody: P09882(PSMA1 Antibody) at dilution 1/800, Secondary antibody: Goat anti rabbit IgG at 1/5000 dilution, Exposure time: 1 second    

  
  

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     The image is immunohistochemistry of paraffin-embedded Human prostate cancer tissue using P09882(PSMA1 Antibody) at dilution 1/160. (Original magnification: ×200)    

  
  

PSMA1 (Proteasome 20S Subunit Alpha 1) is a core component of the 20S proteasome, a multi-subunit complex central to the ubiquitin-proteasome system responsible for regulated protein degradation. As part of the 19S-20S-11S proteasome assemblies, PSMA1 forms the outer α-ring of the 20S catalytic core, facilitating substrate recognition, gate opening, and structural stability. Its role in maintaining cellular proteostasis impacts critical processes like cell cycle progression, stress response, and antigen presentation.

PSMA1 antibodies are essential tools for studying proteasome composition, dynamics, and dysfunction. These antibodies are widely used in techniques such as Western blotting, immunofluorescence, and co-immunoprecipitation to detect PSMA1 expression, localization, and interaction partners. Given the proteasome's involvement in diseases like cancer and neurodegenerative disorders, PSMA1 antibodies help investigate pathological mechanisms, particularly in contexts of proteasome inhibition or overexpression. For instance, elevated PSMA1 levels in certain cancers correlate with drug resistance, making it a potential therapeutic biomarker.

Validated PSMA1 antibodies typically show specificity for the ~30 kDa protein across human and model organisms. Researchers prioritize antibodies verified in knockout controls to avoid cross-reactivity with other α-subunits (PSMA2-7). Commercial variants include monoclonal and polyclonal formats, often conjugated to fluorophores or enzymes for multiplex assays. Recent studies also utilize PSMA1 antibodies in proteasome activity profiling and single-particle cryo-EM structural analyses, underscoring their versatility in both basic and translational research.