FADD Rabbit Polyclonal Antibody

Function

The Fas-associated death domain-containing protein (FADD) was initially identified as an adaptor required for cell death signal transduction initiated by Fas. FADD contains two protein-protein interaction structures: the death domain (DD) at the carboxy terminus and the death effector domain (DED) at the amino terminus. FADD is involved in signaling induced by other DRs such as TNFR-I, TRAIL receptors (or DR4/5), and DR3. Overexpression of FADD causes apoptosis, which can be blocked by the cow pox protein CrmA, suggesting that FADD lies upstream of ICE and possibly other serine proteases.

Background References

1. Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J., Wilming L.G. Hayashizaki Y.;"The transcriptional landscape of the mammalian genome.";Science 309:1559-1563(2005).

2. Zhang J., Winoto A.;"A mouse Fas-associated protein with homology to the human Mort1/FADD protein is essential for Fas-induced apoptosis.";Mol. Cell. Biol. 16:2756-2763(1996).

Post-translational Modification

Phosphorylated.

Subcellular Location

Cell cytosol

UNIPROT

SwissProt: Q61160 Mouse

Synonyms