Purified Mouse Anti-Human TRAF3

TRAF3 (TNF Receptor Associated Factor 3) is a member of a group of putative signal transducing molecules which interact with several members of the TNF receptor family. TRAF3 was discovered based on its interaction with CD40 and the dominant oncogene of Epstein-Barr virus, LMP-1. As such, it also known as CRAF1 and LAP1. TRAF proteins share a novel C-terminal homology region, the "TRAF" domain, as well as an N-terminal Zinc/RING finger and/or multiple Zinc finger motifs. A leucine zipper (coiled coil) region lies between the Zinc/RING finger and TRAF domains and may promote homodimerization and  heterodimerization of TRAF proteins and receptor interaction. In vitro, TRAF3 binds directly to the cytoplasmic domains of CD30, CD40, LT-βR and TNFR type II. TRAF3 has been shown to play a role in intracellular signal  pathways associated with these receptors, including induction of cell death and of the transcription factor, NF-κB. Studies on TRAF3- deficient mice have shown that TRAF3 is required for postnatal development and for normal T-cell function. TRAF3 migrates at a molecular weight of ~64 kDa in SDS/PAGE. The B1-6 antibody recognizes an ~64 kDa band corresponding to human TRAF3. A recombinant human TRAF3 protein fragment corresponding to amino acids 571-620 was used as immunogen.