FAS Ligand Human Recombinant
FAS Ligand Human Recombinant, HEK
sFas Receptor Human Recombinant
sFas Receptor Human Recombinant, His Tag
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.
sFas Receptor Human Recombinant, Sf9
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.
Sf9, Baculovirus cells.
The Fas receptor, also known as Fas, FasR, apoptosis antigen 1 (APO-1 or APT), cluster of differentiation 95 (CD95), or tumor necrosis factor receptor superfamily member 6 (TNFRSF6), is a protein encoded by the FAS gene in humans . It is a death receptor on the surface of cells that leads to programmed cell death (apoptosis) upon binding with its ligand, Fas ligand (FasL) .
Key Biological Properties: The mature Fas protein has 319 amino acids, with a predicted molecular weight of 48 kilodaltons. It is divided into three domains: an extracellular domain, a transmembrane domain, and a cytoplasmic domain .
Expression Patterns: Fas is expressed in various tissues, including lymphoid tissues, bone marrow, and immune cells such as T cells, B cells, and natural killer (NK) cells .
Tissue Distribution: Fas is widely distributed across different tissues, including the liver, lung, kidney, and heart .
Primary Biological Functions: Fas plays a crucial role in inducing apoptosis, a form of programmed cell death. This process is essential for maintaining immune homeostasis and eliminating damaged or infected cells .
Role in Immune Responses: Fas is involved in the regulation of the immune system by controlling the activation-induced cell death (AICD) of T cells, thereby preventing autoimmunity .
Pathogen Recognition: Fas-mediated apoptosis helps in the removal of pathogen-infected cells, contributing to the body’s defense mechanisms .
Mechanisms with Other Molecules and Cells: Fas interacts with its ligand, FasL, to form the death-inducing signaling complex (DISC). This complex recruits the adapter molecule FADD (Fas-associated death domain), which in turn activates caspase-8, leading to a cascade of caspase activation and apoptosis .
Binding Partners: Fas primarily binds with FasL, but it can also interact with other molecules such as FADD and caspase-8 .
Downstream Signaling Cascades: The binding of Fas to FasL triggers the formation of DISC, which activates caspase-8. This activation leads to the cleavage of downstream effector caspases, ultimately resulting in apoptosis .
Transcriptional Regulation: The expression of Fas is regulated by various transcription factors, including NF-κB and p53 .
Post-Translational Modifications: Fas undergoes several post-translational modifications, such as phosphorylation and ubiquitination, which can influence its activity and stability .
Biomedical Research: Fas is extensively studied in the context of cancer, autoimmune diseases, and infectious diseases. It serves as a model for understanding apoptosis and immune regulation .
Diagnostic Tools: Fas and its ligand FasL are used as biomarkers for diagnosing certain cancers and autoimmune disorders .
Therapeutic Strategies: Targeting the Fas-FasL pathway has potential therapeutic applications in treating cancers, autoimmune diseases, and transplant rejection .
Development: Fas-mediated apoptosis is essential during embryonic development for the removal of unwanted cells .
Aging: The regulation of Fas expression and activity changes with age, influencing the aging process and the development of age-related diseases .
Disease: Dysregulation of the Fas-FasL pathway is associated with various diseases, including cancers, autoimmune disorders, and neurodegenerative diseases .