FADD (Fas (TNFRSF6)-associated via death domain)

Polyclonal antibody produced in rabbits immunized with a synthetic peptide corresponding to a region of mouse Fadd.

Suggested starting concentrations are provided. Optimal dilutions should be determined by end-user. Differences in calculated versus apparent molecular weight may be due to post-translational modifications or protein hydrophobicity. Fadd is apoptotic adaptor molecule that recruits caspase-8 or caspase-10 to the activated Fas (CD95) or TNFR-1 receptors. The resulting aggregate called the death-inducing signaling complex (DISC) performs caspase-8 proteolytic activation. Active caspase-

Interacts with CFLAR PEA15 and MBD4. When phosphorylated part of a complex containing HIPK3 and FAS. May interact with MAVS/IPS1. Interacts with LRDD (By similarity).

Phosphorylated.

Contains 1 DED (death effector) domain. [1] Zhande R. Dauphinee S. M. Thomas J. A. Yamamoto M. Akira S. and Karsan A. FADD negatively regulates lipopolysaccharide signaling by impairing interleukin-1 receptor-associated kinase 1-MyD88 interaction[2] Osborn S. L. Sohn S. J. and Winoto A. et al. Constitutive phosphorylation mutation in Fas-associated death domain (FADD) results in early cell cycle defects[3] Luedde T. Beraza N. Kotsikoris V. van Loo G. Nenci A. De Vos R. Roskams T. Trautwein C. and Pasparakis M. Deletion of NEMO/IKKgamma in liver parenchymal cells causes steatohepatitis and hepatocellular carcinoma[4] O\' Flaherty J. Mei Y. Freer M. and Weyman C. M. et al. Signaling through the TRAIL receptor DR5/FADD pathway plays a role in the apoptosis associated with skeletal myoblast differentiation[5] Imtiyaz H. Z. Rosenberg S. Zhang Y. Rahman Z. S. Hou Y. J. Manser T. and Zhang J. The Fas-associated death domain protein is required in apoptosis and TLR-induced proliferative responses in B cells[6] Zhang J. Winoto A. A mouse Fas-associated protein with homology to the human Mort1/FADD protein is essential for Fas-induced apoptosis. [7] Hsu H. Shu H. -B. Pan M. G. Goeddel D. V. TRADD-TRAF2 and TRADD-FADD interactions define two distinct TNF receptor 1 signal transduction pathways. [8] Carninci P. Kasukawa T. Katayama S. Gough J. Frith M. C. Maeda N. Oyama R. Ravasi T. Lenhard B. Wells C. et al. The transcriptional landscape of the mammalian genome. [9] Jeong E. -J. Bang S. Lee T. H. Park Y. -I. Sim W. -S. Kim K. -S. The solution structure of FADD death domain. Structural basis of death domain interactions of Fas and FADD.