The FAS Blocking Antibody, also known as CD95, is a monoclonal antibody derived from mice and is specifically designed to target human FAS (CD95) proteins. This antibody plays a crucial role in the study of apoptosis, a form of programmed cell death, by inhibiting the interaction between FAS and its ligand, FASL. This interaction is essential for the induction of apoptosis in various cell types.
FAS, also known as CD95 or APO-1, is a cell surface receptor that belongs to the tumor necrosis factor (TNF) receptor superfamily. It is a 45 kDa type I transmembrane glycoprotein that is widely expressed in various tissues. The primary function of FAS is to mediate apoptosis through its interaction with FAS ligand (FASL), a process that is critical for maintaining immune system homeostasis and eliminating harmful or unnecessary cells .
The FAS receptor, upon binding with its ligand FASL, undergoes trimerization and recruits adaptor proteins such as FADD (FAS-associated death domain). This recruitment leads to the formation of the death-inducing signaling complex (DISC), which subsequently activates caspases, the proteases responsible for the execution of apoptosis . The FAS Blocking Antibody inhibits this interaction, thereby preventing the initiation of the apoptotic cascade.
The FAS Blocking Antibody has several applications in research and clinical settings:
The FAS Blocking Antibody is produced by immunizing mice with recombinant human FAS protein. The resulting hybridoma cells are screened for the production of antibodies that specifically bind to human FAS and block its interaction with FASL. The antibody is typically purified from the hybridoma cell culture supernatant using protein A or G affinity chromatography .
Key characteristics of the FAS Blocking Antibody include: