Human TRAF-1 Antibody

Tumor Necrosis Factor (TNF) Receptor-Associated Factors (TRAFs) are a family of adaptor proteins that interact with a wide range of cell surface receptors and participate in the regulation of cell survival, proliferation, differentiation, and stress response. TRAFs were identified by their ability to form complexes with TNF receptor superfamily members but more recently are reported to also bind to Toll/IL-1 receptor family members and mediate cellular signaling. Six members of the TRAF family have been identified. All TRAF proteins have a homologous C-terminal TRAF domain that can bind the cytoplasmic domain of receptors as well as other TRAFs. TRAF-1, also known as EBI6, is a 416 amino acid, 46 kDa protein that is a unique member of the TRAF family, in that it lacks the N-terminal RING finger domain common in TRAFs 2-6. TRAF-1 interacts with the cytoplasmic domain of TNFR2 and other TNFR family members to mediate downstream signaling events. TRAF-1 is a substrate for caspases activated by TNF family death receptors. TRAF-1 can homodimerize as well as form heterodimers with TRAF-2.