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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). The Fas ligand (Fas ligand, FasL, CD95L) is an integral membrane protein and is a type II transmembrane glycoprotein. FasL is a member of the TNF family, which includes TNFa, a- and b-chains of lymphotoxin (LT), CD40 ligand and CD30 ligand. The action of Fas is mediated via FADD (Fas-associated death domain)/MORT1, an adapter protein that has a death domain at its C-terminus and binds to the cytoplasmic death domain of Fas.
Monoclonal Antibodies to Fas Ligand (CD95L)
Immunogen: recombinant soluble active extracellular domain of human Fas ligand. Purified from culture supernatant of hybridoma cells, grown in a bioreactor.
Applications: ELISA, immunoprecipitation, immunocytochemistry and flow cytometry.
Monoclonal Anti-Fas (CD95/Apo-1)
Immunogen: murine L cells transfected by a human Fas/CD95 cDNA. Purified from culture supernatant of hybridoma cells grown in a bioreactor.
Applications: immunoblotting, flow cytometry and the induction of apoptosis.
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