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Description
Ultra-LEAF? Purified anti-CD95 (Fas). FAS was initially purified and cloned from SKW6.4 cells and a cDNA library of human T cell lymphoma KT-3 cells.? FAS is a type I transmembrane protein and belongs to the TNF receptor superfamily. The extracellular region of the FAS possesses three cystein-rich domains characteristic of the TNF superfamily, and the intracellular region includes a death domain (DD). The binding of FASL to FAS induces conformational changes in FAS, leading to recruitment of FADD and procaspase-8, and assembly of the death-inducing signalling complex (DISC). Subsequently, caspase 8 is released from DISC and induces activation of caspase 3 and 7, proteolysis of cellular components, and apoptosis. Biological effects not based on apoptotic cell death have also been described. The interaction of FAS/FASL in immature dendritic cells (DCs) induces functional maturation. Fas-activated DCs increase the expression of MHC II, B7 co-stimulatory molecules, and DC–lysosome-associated membrane protein (DC-LAMP), and secrete proinflammatory cytokines such as IL-1β and TNF-α. In addition, FAS/FASL interaction increases the production of chemokines in NK-T cells, and FASL acts as a survival factor for human CD34+ cells and increases their colony formation. Human activated PBMC and tumor cell lines express full-length mRNA and several mRNA FAS variants derived by alternative splicing; deletion of an exon encoding the transmembrane domain results in a soluble FAS molecule that blocks apoptosis. Patients with systemic lupus erythematosus show high levels of soluble FAS.