TRAF6 (Tumor Necrosis Factor Receptor-Associated Factor 6) is a crucial adaptor protein involved in multiple signaling pathways, including NF-κB and MAPK activation, which regulate immune responses, inflammation, and cell survival. As a member of the TRAF family, TRAF6 functions as an E3 ubiquitin ligase, facilitating the assembly of signaling complexes through K63-linked polyubiquitination. It mediates signals from receptors like Toll-like receptors (TLRs), interleukin-1 receptor (IL-1R), and the TNF receptor superfamily, linking extracellular stimuli to intracellular signaling cascades.
TRAF6 antibodies are essential tools for studying its expression, post-translational modifications, and interactions in various biological contexts. These antibodies are widely used in techniques such as Western blotting, immunoprecipitation, immunofluorescence, and immunohistochemistry to investigate TRAF6's role in diseases like cancer, autoimmune disorders, and infectious diseases. Researchers rely on TRAF6-specific antibodies to assess its activation status, subcellular localization, and association with downstream effectors under different experimental conditions. Validated antibodies typically target conserved regions, such as the TRAF-C domain or N-terminal zinc-binding motifs, ensuring specificity across human, mouse, and rat samples. Quality control involves testing in knockout models or siRNA-treated cells to confirm minimal cross-reactivity. As dysregulated TRAF6 signaling is implicated in pathological processes, its antibodies also support drug discovery efforts targeting inflammatory and oncogenic pathways.