FAS Human, Sf9
Sf9, Baculovirus cells.
Tumor necrosis factor receptor superfamily member 6, Apo-1 antigen, Apoptosis-mediating surface antigen FAS, FASLG receptor, CD95, FAS, APT1, FAS1, APO-1, FASTM, ALPS1A, TNFRSF6.
Greater than 95.0% as determined by SDS-PAGE.
Description
FAS Human Recombinant produced in Baculovirus is a single glycosylated polypeptide chain containing 156 amino acids (26-173 aa) and having a molecular mass of 17.7KDa.
FAS is fused to a 8 amino acid His-Tag at C-terminus and purified by proprietary chromatographic techniques.
Product Specs
FAS, also known as tumor necrosis factor receptor superfamily member 6 (TNFRSF6), belongs to the death receptor family within the TNF receptor protein family. This protein plays a critical role in regulating viral infections. FAS is expressed in virtually all cell types, while its corresponding ligand, FasL, is found in activated T cells, natural killer (NK) cells, and dendritic cells. The regulation of FasL and TRAIL on human cytomegalovirus (HCMV)-infected dendritic cells enhances the direct elimination of activated T lymphocytes. Moreover, the activation of FasL in HCMV-infected retinal pigment epithelial cells can contribute to the impairment of neutrophil function in HCMV retinitis.
Recombinant human FAS protein, expressed in Baculovirus, is a single glycosylated polypeptide chain. It consists of 156 amino acids (spanning residues 26-173) and has a molecular weight of 17.7 kDa. The protein includes an 8-amino acid His-tag fused at the C-terminus. Purification is achieved through proprietary chromatographic techniques.
The FAS protein solution has a concentration of 0.5 mg/ml. It is formulated in a solution containing 10% glycerol and Phosphate-Buffered Saline (PBS) at a pH of 7.4.
For short-term storage (up to 2-4 weeks), the product can be stored at 4°C. For extended storage, it is recommended to freeze the product at -20°C. To ensure optimal stability during long-term storage, adding a carrier protein (such as 0.1% HSA or BSA) is advisable. It's important to avoid repeated cycles of freezing and thawing.
The purity of the FAS protein is determined to be greater than 95.0% using SDS-PAGE analysis.
Tumor necrosis factor receptor superfamily member 6, Apo-1 antigen, Apoptosis-mediating surface antigen FAS, FASLG receptor, CD95, FAS, APT1, FAS1, APO-1, FASTM, ALPS1A, TNFRSF6.
Sf9, Baculovirus cells.
QVTDINSKGL ELRKTVTTVE TQNLEGLHHD GQFCHKPCPP GERKARDCTV NGDEPDCVPC QEGKEYTDKA HFSSKCRRCR LCDEGHGLEV EINCTRTQNT KCRCKPNFFC NSTVCEHCDP CTKCEHGIIK ECTLTSNTKC KEEGSRSNLE HHHHHH
Product Science Overview
The sFas receptor, also known as the soluble Fas receptor, is a member of the tumor necrosis factor receptor superfamily (TNFRSF6). It is also referred to by several other names, including CD95, Apo-1 antigen, and apoptosis-mediating surface antigen Fas . The sFas receptor plays a crucial role in the regulation of programmed cell death (apoptosis), which is essential for maintaining cellular homeostasis and immune system function.
The human recombinant sFas receptor produced in Sf9 cells is a single glycosylated polypeptide chain containing 156 amino acids (26-173 aa) with a molecular mass of approximately 17.7 kDa . The receptor is fused to an 8 amino acid His-Tag at the C-terminus, which facilitates its purification using proprietary chromatographic techniques . The recombinant protein is produced using the baculovirus expression system in Sf9 insect cells, which allows for high-yield production and proper post-translational modifications.
The sFas receptor is involved in the extrinsic pathway of apoptosis. It binds to its cognate ligand, FasL (Fas ligand), which is expressed on the surface of activated T cells, natural killer (NK) cells, and dendritic cells . Upon binding to FasL, the sFas receptor undergoes a conformational change that triggers the formation of the death-inducing signaling complex (DISC). This complex subsequently activates caspases, which are proteolytic enzymes that execute the apoptotic program by cleaving various cellular substrates .
The recombinant sFas receptor has several applications in research and therapeutic development. It is used to study the mechanisms of apoptosis and to investigate the role of Fas/FasL interactions in various diseases, including cancer, autoimmune disorders, and viral infections . Additionally, the sFas receptor is utilized in drug screening assays to identify potential therapeutic agents that can modulate apoptosis pathways.
The sFas receptor is supplied as a sterile filtered colorless solution containing 10% glycerol and phosphate-buffered saline (pH 7.4) . For short-term storage, it can be kept at 4°C if used within 2-4 weeks. For long-term storage, it is recommended to store the protein at -20°C with the addition of a carrier protein (0.1% HSA or BSA) to prevent degradation . It is important to avoid multiple freeze-thaw cycles to maintain the protein’s stability and activity.
