TRIM27 (Tripartite Motif-Containing 27), also known as RFP (Ret Finger Protein), is a member of the TRIM protein family characterized by its conserved N-terminal RING, B-box, and coiled-coil domains. It functions as an E3 ubiquitin ligase, playing roles in ubiquitination, transcriptional regulation, and cellular processes such as apoptosis, immune response, and carcinogenesis. TRIM27 is implicated in various diseases, including cancers, where it may act as an oncogene by promoting cell proliferation, inhibiting apoptosis, or modulating signaling pathways like Wnt/β-catenin and NF-κB. It also interacts with viral proteins, influencing antiviral responses.
TRIM27 antibodies are essential tools for studying its expression, localization, and molecular interactions. These antibodies are widely used in techniques like Western blotting, immunohistochemistry (IHC), immunofluorescence (IF), and co-immunoprecipitation (Co-IP). High-quality TRIM27 antibodies exhibit specificity for distinct epitopes, enabling the detection of endogenous TRIM27 across human, mouse, and rat samples. Researchers rely on them to explore TRIM27's role in tumor progression, immune regulation, and neurodegenerative disorders. Validation via knockout cell lines or siRNA knockdown ensures antibody reliability. Commercial TRIM27 antibodies are typically developed in hosts like rabbit or mouse, with formats ranging from purified IgG to conjugated variants for advanced imaging or flow cytometry applications.