TRIM15 (Tripartite Motif-containing protein 15) is a member of the TRIM family, a group of proteins characterized by conserved RING, B-box, and coiled-coil domains. These proteins are involved in diverse cellular processes, including innate immunity, antiviral defense, and autophagy. TRIM15. specifically, has been implicated in regulating immune signaling pathways and viral restriction. Studies suggest it acts as an E3 ubiquitin ligase, mediating protein ubiquitination to influence processes like NF-κB and MAPK signaling. It also exhibits antiviral activity against certain viruses, including HIV-1. by targeting viral capsids or interfering with viral replication cycles.
TRIM15 antibodies are essential tools for studying the protein's expression, localization, and functional roles. They enable detection of TRIM15 in various experimental setups, such as Western blotting, immunofluorescence, and immunoprecipitation. These antibodies are particularly valuable in research exploring innate immune responses, host-pathogen interactions, and TRIM15's potential involvement in diseases like autoimmune disorders or cancers. Validation of TRIM15 antibodies typically includes testing for specificity using knockout cell lines or siRNA-mediated knockdown to ensure minimal cross-reactivity with other TRIM family members. Recent studies also highlight its role in regulating inflammasome activation and cytokine production, further emphasizing its relevance in inflammatory and infectious disease contexts.