TRADD (TNF Receptor Associated Death domain) is an ~36 kDa protein that interacts specifically with the cytoplasmic domain of the type I TNF Receptor. Overexpression of the C-terminal 118 amino acids of TRADD, the "death domain," is sufficient to induce two major TNF-induced responses, apoptosis and activation of nuclear transcription factor, NF-κB. Evidence suggests that TRADD interacts with other signal molecules including TRAF1, TRAF2 and FADD, allowing recruitment of these molecules to the TNF receptor complex. A similar interaction has been demonstrated for TRADD and the serine/threonine kinase RIP. Coexpression of the ICE-specific protease inhibitor, CrmA, inhibits TRADD-induced apoptosis, but does not affect induction of NF-κB, suggesting that TRADD may serve to initiate distinct signal pathways.
The B36-2 antibody recognizes an ~36 kDa band corresponding to human TRADD. A recombinant human TRADD protein fragment corresponding to amino acids 14-62 was used as immunogen.