Human TRAF‑2 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. TRAFs 2‑6 have N-terminal RING and zinc finger domains that are involved in signaling downstream events. TRAF-2, also known as TNF Receptor-Associated Protein (TRAP), is a 501 amino acid, 56 kDa protein which interacts with the cytoplasmic domain of TNFR1, TNFR2 and CD40 to mediate the activation of NF-kappa-B and AP-1 family of transcription factors. TRAF-2 can self-associate as well as form heterodimers with TRAF-1.