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During apoptosis, cells exhibit morphological signs of the death process: cell shrinkage, membrane blebbing, and chromatin condensation. The role of the cell surface cytokine receptor, Fas (Apo-1, CD95), in apoptosis has been well characterized. The tumor necrosis factor receptor (TNF-R) can trigger cell death, as well as various other responses. Data suggested that Fas and TNF-R affect a common target in the cell death pathway. This target has been identified as FADD, a novel protein that contains a death domain homologous to the death domains of Fas and TNF-R1. FADD specifically binds to Fas, an association mediated by their homologous death domains. Overexpression of FADD induces apoptosis that is inhibited by CrmA, a poxvirus protein that blocks both Fas- and TNF-induced cell death. Thus, FADD is a central element of the Fas-mediated cell death pathway. This antibody is routinely tested by western blot analysis. Other applications were tested at BD Biosciences Pharmingen during antibody development only or reported in the literature.
