|Detection of Human/Mouse/Rat TRAF‑3 Isoform 2 by Western Blot. Western blot shows lysates of HeLa human cervical epithelial carcinoma cell line, A20 mouse B cell lymphoma cell line, and Rat‑2 rat embryonic fibroblast cell line. PVDF membrane was probed with 2 µg/mL of Human/Mouse/Rat TRAF‑3 Isoform 2 Monoclonal Antibody (Catalog # MAB3278) followed by HRP‑conjugated Anti-Rat IgG Secondary Antibody (Catalog # HAF005). A specific band was detected for TRAF‑3 Isoform 2 at approximately 65 kDa (as indicated). This experiment was conducted under reducing conditions and using Immunoblot Buffer Group 2.|
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. Seven 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. Two isoforms of TRAF-3 have been identified, a 568 amino acid, 64 kDa protein (isoform 1, also known as CD40BP and CRAF1) and a 543 amino acid, 62 kDa protein (isoform 2, also known as CAP1 and LAP1). TRAF-3 has been shown bind specifically to the PEQET sequence motif on the cytoplasmic domain of CD40. TRAF-3 and TRAF-6 have also been identified as being involved in TLR signaling events.
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