Recombinant Human FADD protein

FADD (Fas-associated protein with death domain) is a pivotal adaptor protein involved in apoptotic signaling pathways and immune regulation. Discovered in the mid-1990s, it plays a central role in transmitting death signals from cell surface death receptors, such as Fas (CD95) and TNF receptor superfamily members, to intracellular caspase cascades. Structurally, FADD contains two conserved domains: an N-terminal death effector domain (DED) that interacts with initiator caspases like caspase-8/10. and a C-terminal death domain (DD) responsible for binding activated death receptors. This bridging function enables FADD to assemble the death-inducing signaling complex (DISC), triggering caspase activation and programmed cell death.

Recombinant FADD protein refers to the engineered version produced using expression systems like *E. coli* or mammalian cells. Its production involves cloning the FADD gene into expression vectors, followed by purification via affinity chromatography. Recombinant technology ensures high purity, specificity, and controlled post-translational modifications, making it invaluable for mechanistic studies. Researchers employ recombinant FADD to investigate apoptosis regulation, necroptosis crosstalk, and immune signaling dynamics in vitro. It also serves as a tool for screening therapeutic compounds targeting cell death pathways in cancer, autoimmune diseases, and neurodegenerative disorders. Recent studies highlight its involvement beyond apoptosis, including inflammasome modulation and T-cell receptor signaling, expanding its biomedical relevance. The availability of recombinant FADD continues to advance our understanding of cell fate decisions and therapeutic interventions in death receptor-mediated pathologies.