Monoclonal Anti-Fas (CD95/Apo-1)−FITC antibody produced in mouse

Many cells can be activated to undergo apoptosis following the interaction of selected ligands with cell surface receptors. The most well studied receptors are CD95/Fas/Apo-1 (apoptosis inducing protein 1) and tumor necrosis factor receptor 1 (TNFR1). Apoptosis mediated by either of these results in activation of the caspases. However, Fas-mediated death occurs much more rapidly than that triggered by TNFR1. Human Fas/CD95/Apo-1 is a single transmembrane glycoprotein receptor (325 amino acids, 45-48 kDa).

murine L cells transfected with a human Fas/CD95 cDNA.

Monoclonal Anti-Fas (CD95/Apo-1)-FITC antibody is suitable for flow cytometry at a dilution of 1:50 using cultured human Burkitt′s lymphoma Raji cells.

APO-1/Fas(CD95) comprises of a death domain (DD) within the cytoplasmic region which triggers apoptosis upon binding of their cognate ligands. Once it is activated, APO-1/Fas(CD95) further aggregates its intracellular death domains which leads to the recruitment of two key signaling proteins followed by the formation of death-inducing signaling complex. These complex crosslinks through its C-terminal DD with APO-1/Fas receptors and engage caspase-8 via its N-terminal death effector domain (DED) to the DISC.

Reacts specifically with the functional epitope of human Fas (CD95/Apo-1) antigen. By immunoblotting, the clone recognizes denatured, non-reduced recombinant human Fas (amino acid residues 1-173). The antibody is reactive in flow cytometry, and may be reactive in the induction of apoptosis.

Solution in 0.01 M phosphate buffered saline, pH 7.4, containing 1% BSA and 15 mM sodium azide.