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Human Fas Ligand/TNFSF6 Protein 4897

$420.00$1,400.00

Summary

  • Expression: HEK293
  • Functional: Yes (ELISA)
  • Amino Acid Range: Pro134-Leu281
SKU: 4897parent Categories: , Tag:
Weight1 lbs
Dimensions9 × 5 × 2 in
accession

AAH17502

express system

HEK293

product tag

N-His

purity

> 95% as determined by Tris-Bis PAGE

background

Fas ligand (FasL, CD95L) is a 40-kDa type II transmembrane protein that binds to Fas (CD95) receptors and promotes programmed cell death. Fas receptors are expressed at higher levels in many tumors than in normal cells.Somewhat paradoxically, elimination of Fas or FasL from tumors also leads to death induced by CD95 receptor/ligand elimination (DICE).

molecular weight

The protein has a predicted MW of 18 kDa. Due to glycosylation, the protein migrates to 20-35 kDa based on Tris-Bis PAGE result.

available size

100 µg, 500 µg

endotoxin

Less than 1EU per μg by the LAL method.

Human Fas Ligand/TNFSF6 Protein 4897

protein
Size and concentration
100, 500µg and lyophilized
Form
Lyophilized
Storage Instructions
Valid for 12 months from date of receipt when stored at -80°C. Recommend to aliquot the protein into smaller quantities for optimal storage. Please minimize freeze-thaw cycles.
Storage buffer
Shipped at ambient temperature.
Purity
> 95% as determined by Tris-Bis PAGE
target relevance
Fas ligand (FasL, CD95L) is a 40-kDa type II transmembrane protein that binds to Fas (CD95) receptors and promotes programmed cell death. Fas receptors are expressed at higher levels in many tumors than in normal cells.Somewhat paradoxically, elimination of Fas or FasL from tumors also leads to death induced by CD95 receptor/ligand elimination (DICE).
Protein names
Tumor necrosis factor ligand superfamily member 6 (Fas antigen ligand) (Fas ligand) (FasL) (CD antigen CD178) [Cleaved into: Tumor necrosis factor ligand superfamily member 6, membrane form; Tumor necrosis factor ligand superfamily member 6, soluble form (Receptor-binding FasL ectodomain) (Soluble Fas ligand) (sFasL); ADAM10-processed Fas
Protein family
Tumor necrosis factor family
Mass
31361Da
Function
Cytokine that binds to TNFRSF6/FAS, a receptor that transduces the apoptotic signal into cells. Involved in cytotoxic T-cell-mediated apoptosis, natural killer cell-mediated apoptosis and in T-cell development. Initiates fratricidal/suicidal activation-induced cell death (AICD) in antigen-activated T-cells contributing to the termination of immune responses. TNFRSF6/FAS-mediated apoptosis has also a role in the induction of peripheral tolerance. Binds to TNFRSF6B/DcR3, a decoy receptor that blocks apoptosis. {ECO:0000250|UniProtKB:P41047, ECO:0000250|UniProtKB:P48023}.; [Tumor necrosis factor ligand superfamily member 6, soluble form]: Induces FAS-mediated activation of NF-kappa-B, initiating non-apoptotic signaling pathways. Can induce apoptosis but does not appear to be essential for this process. {ECO:0000250|UniProtKB:P41047}.; [FasL intracellular domain]: Cytoplasmic form induces gene transcription inhibition. {ECO:0000250|UniProtKB:P48023}.
Subellular location
Cell membrane {ECO:0000250|UniProtKB:P48023}; Single-pass type II membrane protein {ECO:0000255}. Cytoplasmic vesicle lumen {ECO:0000250|UniProtKB:P48023}. Lysosome lumen {ECO:0000250|UniProtKB:P48023}. Note=Colocalizes with the SPPL2A protease at the cell membrane. Is internalized into multivesicular bodies of secretory lysosomes after phosphorylation by FGR and monoubiquitination. {ECO:0000250|UniProtKB:P48023}.; [Tumor necrosis factor ligand superfamily member 6, soluble form]: Secreted {ECO:0000250|UniProtKB:P48023}. Note=May be released into the extracellular fluid by cleavage from the cell surface. {ECO:0000250|UniProtKB:P48023}.; [FasL intracellular domain]: Nucleus {ECO:0000250|UniProtKB:P48023}. Note=The FasL ICD cytoplasmic form is translocated into the nucleus. {ECO:0000250|UniProtKB:P48023}.
Structure
Homotrimer. Interacts with ARHGAP9, BAIAP2L1, BTK, CACNB3, CACNB4, CRK, DLG2, DNMBP, DOCK4, EPS8L3, FGR, FYB1, FYN, HCK, ITK, ITSN2, KALRN, LYN, MACC1, MIA, MPP4, MYO15A, NCF1, NCK1, NCK2, NCKIPSD, OSTF1, PIK3R1, PSTPIP1, RIMBP3C, SAMSN1, SH3GL3, SH3PXD2B, SH3PXD2A, SH3RF2, SKAP2, SNX33, SNX9, SORBS3, SPTA1, SRC, SRGAP1, SRGAP2, SRGAP3, TEC, TJP3 and YES1. {ECO:0000250|UniProtKB:P48023}.
Post-translational modification
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. {ECO:0000250|UniProtKB:P48023}.; Phosphorylated by FGR on tyrosine residues; this is required for ubiquitination and subsequent internalization. {ECO:0000250|UniProtKB:P48023}.; N-glycosylated. Glycosylation enhances apoptotic activity. {ECO:0000250|UniProtKB:P48023}.; Monoubiquitinated. {ECO:0000250|UniProtKB:P48023}.
Target Relevance information above includes information from UniProt accession: Q861W5
The UniProt Consortium

Data

SPR with Human Fas Ligand/TNFSF6 Protein
Human Fas, His Tag immobilized on CM5 Chip can bind Human Fas Ligand, His Tag with an affinity constant of 19.45 nM as determined in SPR assay (Biacore T200).
ELISA with Human Fas Ligand/TNFSF6 Protein
Immobilized Human Fas Ligand, His Tag at 2µg/ml (100µl/Well) on the plate. Dose response curve for Human Fas, hFc Tag with the EC50 of 0.19µg/ml determined by ELISA (QC Test).
SDS-PAGE gel of Human Fas Ligand/TNFSF6 Protein
Human Fas Ligand on Tris-Bis PAGE under reduced condition. The purity is greater than 95%.

Publications

Published literature highly relevant to the biological target of this product and referencing this antibody or clone are retrieved from PubMed database provided by The United States National Library of Medicine at the National Institutes of Health.




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Protocols

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Documents

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