FAS Human
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.
THE BioTek's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
Description
The FAS is purified by proprietary chromatographic techniques.
Product Specs
(a) Analysis using RP-HPLC.
(b) Analysis using SDS-PAGE.
Product Science Overview
The full-length Fas receptor is a type I transmembrane protein composed of 319 amino acids. It includes:
- A 157 amino acid extracellular domain
- A 17 amino acid transmembrane domain
- A 145 amino acid cytoplasmic domain
The recombinant human soluble Fas receptor (sFasR) is a 157 amino acid polypeptide with a molecular weight of approximately 17.6 kDa . This recombinant form corresponds to the TNFR-homologous cysteine-rich extracellular Fas domain and is produced in E. coli .
The Fas receptor and its ligand, FasL, play a pivotal role in inducing apoptosis. When FasL binds to the Fas receptor on the surface of a cell, it triggers a cascade of events leading to cell death. This process involves the recruitment of pro-caspase 8 through an adaptor molecule called FADD (Fas-associated death domain), which then processes the pro-enzyme into its active forms. These active caspases cleave various cellular substrates, ultimately leading to apoptosis .
The soluble Fas receptor (sFasR) acts as a decoy receptor. By binding to FasL, it inhibits FasL-induced apoptosis, effectively serving as a sink for FasL and preventing it from interacting with the membrane-bound Fas receptor .
The biological activity of the recombinant human sFas receptor is determined by its ability to inhibit the cytotoxicity of Jurkat cells. The effective dose (ED50) for this inhibition is between 10-15 µg/ml in the presence of 2 ng/ml of human FasL .
Due to its role in regulating apoptosis, the sFas receptor is of significant interest in research related to the immune system, cancer, and autoimmune diseases. It is also studied in the context of AIDS/HIV and other conditions where apoptosis plays a critical role .
The recombinant human sFas receptor is produced using proprietary chromatographic techniques to ensure high purity. It is non-glycosylated and has a purity level of ≥ 98% as determined by SDS-PAGE gel and HPLC analyses . The endotoxin level is maintained at less than 0.1 ng/µg of protein, ensuring its suitability for research applications .
