Fas and Fas Ligand (FasL) belong to the TNF superfamily and are type I and type II transmembrane proteins, respectively. Binding of FasL to Fas triggers apoptosis in Fas-bearing cells. The mechanism of apoptosis involves recruitment of pro-caspase 8 through an adaptor molecule called FADD followed by processing of the pro-enzyme to active forms. These active caspases then cleave various cellular substrates leading to the eventual cell death. sFasR is capable of inhibiting FasL-induced apoptosis by acting as a decoy receptor that serves as a sink for FasL. The full length Fas (receptor) is a 319 amino acid type I transmembrane protein, which contains a 157 amino acid extracellular domain, a 17 amino acid transmembrane domain, and 145 amino acid cytoplasmic domain. Recombinant human soluble Fas (sFas Receptor) is a 157 amino acid polypeptide (17.6 kDa) corresponding to the TNFR homologous cysteine rich extracellular domain Fas.
Human FAS expressed in E.coli
CAT# CSC-CTK0497-20 (20 μg); CAT# CSC-CTK0497-100 (100 μg)
Greater than 98% as determined by SDS-PAGE and HPLC analysis.
The ED50 was determined by its ability to inhibit the cytotoxicity of Jurkat cells is between 10-15 μg/ml in the presence of 2 ng/ml of hFasL.
Less than 1 EU/μg.
Lyophilized (freeze-dried), sterile powder. Lyophilized with no additives.
Please centrifuge product briefly before opening vial. The lyophilized protein should be reconstituted in sterile, ultra-pure water to a concentration of 0,1 - 1,0 mg/ml. This solution can then be diluted into other aqueous buffers and stored at -20°C for future use.
Storage & Stability
The lyophilized protein, though stable at room temperature for up to 3 weeks, is best stored desiccated at -20°C. Reconstituted rHu sFasR should be used immediately or stored long-term in undiluted working aliquots at -20°C. Avoid repeated freeze-thaw cycles.
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