Anti-Hu CD95 Purified FAS Monoclonal Antibody

CD95 (Fas, APO-1), a 46 kDa transmembrane glycoprotein, is a cell death receptor of the TNFR superfamily. Stimulation of CD95 results in aggregation of its intracellular death domains, formation of the death-inducing signaling complex (DISC) and activation of caspases. In type I cells caspase 3 is activated by high amounts of caspase 8 generated at the DISC, in type II cells low concentration of caspase 8 activates pathway leading to the release of cytochrome c from mitochondria and activation of caspase 3 by cytochom c. Besides its roles in induction of apoptosis, Fas also triggers pro-inflammatory cytokine responses.

HUT-78 human T cell lymphoma cell line. The antibody LT95 reacts with an extracellular epitope on CD95 (Fas/APO-1), a 46 kDa single chain type I glycoprotein of the tumour necrosis factor/nerve growth factor (TNF/NGF) receptor superfamily, expressed on a variety of normal and neoplastic cells. It seems that the antibody LT95 does not induce Fas mediated apoptosis, although it cross-blocks anti-Fas DX2 antibody that recognizes a functional epitope of Fas molecule.

Isoform 1 and isoform 6 are expressed at equal levels in resting peripheral blood mononuclear cells. After activation there is an increase in isoform 1 and decrease in the levels of isoform 6.

Receptor for TNFSF6/FASLG. The adapter molecule FADD recruits caspase-8 to the activated receptor. The resulting death- inducing signaling complex (DISC) performs caspase-8 proteolytic activation which initiates the subsequent cascade of caspases (aspartate-specific cysteine proteases) mediating apoptosis. FAS- mediated apoptosis may have a role in the induction of peripheral tolerance, in the antigen-stimulated suicide of mature T-cells, or both. The secreted isoforms 2 to 6 block apoptosis (in vitro) .