TRIM25 (Tripartite motif-containing 25) is a member of the TRIM family of proteins, characterized by a conserved N-terminal RBCC motif (RING, B-box, and coiled-coil domains) and a C-terminal PRY/SPRY domain. It functions as an E3 ubiquitin ligase, playing critical roles in innate immunity, antiviral defense, and cellular processes like proliferation and apoptosis. TRIM25 gained prominence for its role in the RIG-I-mediated antiviral signaling pathway, where it catalyzes K63-linked ubiquitination of RIG-I, enabling its interaction with MAVS and triggering type I interferon production. Dysregulation of TRIM25 has been implicated in viral infections, cancers (e.g., breast and ovarian cancers), and autoimmune disorders, with studies highlighting both oncogenic and tumor-suppressive functions depending on cellular context.
Antibodies targeting TRIM25 are essential tools for investigating its expression, post-translational modifications, and interactions. They are widely used in techniques such as Western blotting, immunoprecipitation, immunofluorescence, and chromatin immunoprecipitation (ChIP). Commercial TRIM25 antibodies are typically raised against specific epitopes (e.g., human TRIM25 amino acids 50-150 or 400-500) and available in monoclonal (e.g., clone 1D4. 3A5) or polyclonal formats from hosts like rabbit or mouse. Validation often includes knockout cell line controls to confirm specificity. Research applications span virology (e.g., influenza, Zika virus studies), cancer biology (analyzing TRIM25's dual role in tumor progression), and immune signaling pathways. Key studies utilizing these antibodies have clarified TRIM25's structural domains, its competition with SARS-CoV-2 Nsp1 for RIG-I binding, and its interaction with RNA or proteins like ZAP or Ago2 in gene silencing.