TRIM65 (Tripartite Motif-containing 65) is a member of the TRIM protein family, characterized by conserved RING, B-box, and coiled-coil domains. It functions as an E3 ubiquitin ligase, regulating protein ubiquitination and degradation, and is involved in diverse cellular processes, including immune response, apoptosis, and tumorigenesis. Research highlights its dual roles in cancer: it acts as an oncogene in certain contexts (e.g., promoting lung adenocarcinoma progression via miRNA regulation) or a tumor suppressor (e.g., inhibiting glioblastoma by targeting c-Myc). TRIM65 also interacts with viral RNA during infections, modulating antiviral signaling pathways. Antibodies targeting TRIM65 are essential tools for studying its expression, localization, and molecular mechanisms in diseases. They are widely used in techniques like Western blotting, immunohistochemistry, and immunofluorescence. Commercial TRIM65 antibodies are typically validated for specificity against epitopes within its N-terminal or C-terminal regions. However, variability in antibody performance across experimental conditions (e.g., tissue types or post-translational modifications) necessitates careful validation. Dysregulation of TRIM65 has been implicated in autoimmune disorders and neurological conditions, making it a potential biomarker or therapeutic target. Ongoing studies aim to clarify its context-dependent functions and regulatory networks.