Recombinant Human Fas Ligand Protein
Be the first to review this product! Submit a review
|
(0 Publication)
Recombinant Human Fas Ligand Protein is a Human Fragment protein, in the 134 to 281 aa range, expressed in HEK 293 cells, <0.005 EU/µg endotoxin level, suitable for SDS-PAGE.
View Alternative Names
CD178, APT1LG1, CD95L, FASL, TNFSF6, FASLG, Tumor necrosis factor ligand superfamily member 6, Apoptosis antigen ligand, CD95 ligand, Fas antigen ligand, APTL, CD95-L, Fas ligand, FasL
Reactivity data
Sequence info
Properties and storage information
Shipped at conditions
Appropriate short-term storage conditions
Appropriate long-term storage conditions
Specifications
Form
Lyophilized
Additional notes
SDS PAGE>=95% Purity
General info
Function
Cytokine that binds to TNFRSF6/FAS, a receptor that transduces the apoptotic signal into cells (PubMed : 26334989, PubMed : 9228058). Involved in cytotoxic T-cell-mediated apoptosis, natural killer cell-mediated apoptosis and in T-cell development (PubMed : 7528780, PubMed : 9228058, PubMed : 9427603). Initiates fratricidal/suicidal activation-induced cell death (AICD) in antigen-activated T-cells contributing to the termination of immune responses (By similarity). TNFRSF6/FAS-mediated apoptosis has also a role in the induction of peripheral tolerance (By similarity). Binds to TNFRSF6B/DcR3, a decoy receptor that blocks apoptosis (PubMed : 27806260).. Tumor necrosis factor ligand superfamily member 6, soluble form. Induces FAS-mediated activation of NF-kappa-B, initiating non-apoptotic signaling pathways (By similarity). Can induce apoptosis but does not appear to be essential for this process (PubMed : 27806260).. FasL intracellular domain. Cytoplasmic form induces gene transcription inhibition.
Sequence similarities
Belongs to the tumor necrosis factor family.
Post-translational modifications
The soluble form derives from the membrane form by proteolytic processing. The membrane-bound form undergoes two successive intramembrane proteolytic cleavages. The first one is processed by ADAM10 producing an N-terminal fragment, which lacks the receptor-binding extracellular domain. This ADAM10-processed FasL (FasL APL) remnant form is still membrane anchored and further processed by SPPL2A that liberates the FasL intracellular domain (FasL ICD). FasL shedding by ADAM10 is a prerequisite for subsequent intramembrane cleavage by SPPL2A in T-cells.. N-glycosylated (PubMed:9228058). Glycosylation enhances apoptotic activity (PubMed:27806260).. Phosphorylated by FGR on tyrosine residues; this is required for ubiquitination and subsequent internalization.. Monoubiquitinated.
Subcellular localisation
Lysosome lumen
Target data
Product promise
Please note: All products are 'FOR RESEARCH USE ONLY. NOT FOR USE IN DIAGNOSTIC OR THERAPEUTIC PROCEDURES'.
For licensing inquiries, please contact partnerships@abcam.com