FAS Human, His
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.
Description
Recombinant FAS antigen/ CD95 purified from E. coli is a single non-glycosilated polypeptide chain containing amino acids 157-335 of Fas antigen. The recombinant CD95 is fused to C-terminal 6-histidine amino acids. The FAS antigen is purified by proprietary chromatographic techniques.
Product Specs
Product Science Overview
The sFas receptor is a membrane-bound protein that, upon binding with its ligand FasL (Fas Ligand), triggers a cascade of intracellular signaling events leading to apoptosis. This process is essential for the removal of infected, damaged, or cancerous cells, thus preventing the development of various diseases.
The recombinant human sFas receptor with a His tag is a laboratory-engineered version of the natural receptor. The His tag, a sequence of histidine residues, is added to facilitate purification and detection of the protein. This recombinant protein is produced using various expression systems, such as E. coli or mammalian cells, to ensure proper folding and functionality.
The recombinant sFas receptor is widely used in biomedical research to study apoptosis and related pathways. It serves as a valuable tool for:
- Investigating Apoptosis Mechanisms: Researchers use the recombinant sFas receptor to understand the molecular mechanisms underlying apoptosis and how dysregulation of this process contributes to diseases like cancer and autoimmune disorders.
- Drug Development: The sFas receptor is a target for developing therapeutic agents that can modulate apoptosis. By studying the interaction between the receptor and potential drugs, scientists aim to create treatments that can either promote or inhibit cell death as needed.
- Diagnostic Tools: The recombinant receptor can be used in diagnostic assays to detect abnormalities in apoptosis pathways, aiding in the diagnosis of diseases associated with defective cell death mechanisms.
