Recombinant Human TRAF5 protein

TRAF5 (Tumor Necrosis Factor Receptor-Associated Factor 5) is a member of the TRAF protein family, which plays critical roles in intracellular signaling pathways, particularly those mediated by the TNF receptor superfamily and other immune-related receptors. Structurally, TRAF5 contains a conserved C-terminal TRAF domain responsible for protein-protein interactions, a central coiled-coil region, and an N-terminal RING finger domain that may contribute to its E3 ubiquitin ligase activity. It shares homology with TRAF3 and TRAF2 but exhibits distinct functional characteristics.

Functionally, TRAF5 acts as an adaptor protein, bridging cell surface receptors and downstream signaling components. It is involved in regulating NF-κB and MAPK pathways, which influence immune responses, cell survival, and inflammation. TRAF5 interacts with receptors such as CD40. OX40. and TL1A-DR3. modulating signals in lymphocytes and antigen-presenting cells. Studies suggest TRAF5 can both synergize and antagonize signals from other TRAF proteins, adding complexity to its regulatory roles. For example, it may compete with TRAF2 or TRAF6 for receptor binding, fine-tuning immune activation thresholds.

Recombinant TRAF5 protein is typically produced using bacterial (e.g., E. coli) or mammalian expression systems to preserve post-translational modifications. Purification often involves affinity tags (His, GST) for isolation. This recombinant tool enables in vitro studies of TRAF5-receptor interactions, ubiquitination mechanisms, and pathway crosstalk. Researchers employ it to dissect signaling dynamics, characterize mutations linked to immune dysregulation, and develop inhibitors for autoimmune or neoplastic diseases. Its role in balancing immune tolerance and activation makes TRAF5 a potential therapeutic target, with recombinant forms essential for mechanistic and drug discovery studies.