Cayman Soluble Fas Ligand/CD95 Ligand (human, recombinant; aa 134-281)

Fas ligand (FasL), also known as CD95L, is a type II transmembrane protein and member of the TNF superfamily.¹ It is composed of a cytoplasmic domain, transmembrane domain, stalk region, TNF homology domain (THD), which is involved in homotrimerization, and Fas-binding domain. FasL is expressed in activated T cells, as well as the placenta, testis, lung, prostate, esophagus, uterus and spleen.² Binding of FasL to its receptor Fas leads to formation of a death-inducing signaling complex (DISC) composed of CD95 oligomers, the Fas-associated death domain protein (FADD), and procaspase-8, procaspase-10, and cellular FLICE-like inhibitory protein (c-FLIP), which induces apoptosis.³ Soluble FasL (sFasL) is produced by proteolytic cleavage of FasL by various matrix metalloproteinases (MMPs) and either inhibits FasL-induced apoptosis or induces apoptosis in a context-dependent manner.^1,4 sFasL induces migration of isolated human neutrophils and apoptosis in primary human distal lung epithelial cells.^5,6 It decreases ankylosis in a rat model of collagen-induced arthritis.⁷ Serum levels of sFasL are increased in patients with insulin-dependent diabetes mellitus, systemic lupus erythematosus (SLE), rheumatoid arthritis, gastric cancer, or leukemia. Cayman’s Soluble Fas Ligand/CD95 Ligand (human, recombinant; aa 134-281) protein can be used for binding assays. This protein consists of 168 amino acids and has a calculated molecular weight of 19.3 kDa. By SDS-PAGE, under reducing conditions, the apparent molecular mass of the protein is 26 kDa due to glycosylation.

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