The Fas-Associated Death Domain (FADD) is a crucial adaptor protein involved in the transduction of apoptotic signals from death receptors (DRs) to initiate programmed cell death. This protein plays a significant role in maintaining cellular homeostasis by eliminating damaged, infected, or unwanted cells. FADD is also known as MORT1 and is encoded by the FADD gene located on chromosome 11 in humans . The mouse anti-human FADD antibody is commonly used in research to study the protein’s function and its role in various cellular processes.
FADD is a 23 kDa protein composed of 208 amino acids. It contains two main domains: the C-terminal death domain (DD) and the N-terminal death effector domain (DED). These domains, although structurally similar, have distinct functions. The DD of FADD binds to the DD of death receptors such as the Fas receptor, while the DED interacts with the DED of intracellular molecules like procaspase-8 .
Upon ligand binding to the Fas receptor, the receptor trimerizes, and FADD binds to the DD of this trimeric structure. This interaction unmask FADD’s DED, allowing it to recruit procaspase-8 and -10, forming the death-inducing signaling complex (DISC). The activation of these procaspases initiates the caspase cascade, leading to apoptosis .
FADD is predominantly known for its role in apoptosis, but it also participates in other cellular processes such as cell proliferation, autophagy, necroptosis, and inflammation. The protein’s involvement in these processes highlights its versatility and importance in regulating cell survival and proliferation .
The mouse anti-human FADD antibody is widely used in research to study the protein’s function and its role in various cellular processes. This antibody is particularly useful in immunohistochemistry, Western blotting, and flow cytometry to detect and quantify FADD expression in different cell types and tissues.