Recombinant Rat Fas/TNFRSF6/CD95 Fc Chimera Protein, CF Summary
Details of Functionality
Measured by its ability to inhibit Fas Ligand-induced apoptosis of Jurkat human acute T cell leukemia cells. Cheng, J. et al. (1994) Science 263:1759. The ED50 for this effect is 0.05-0.25 µg/mL in the presence of 100 ng/mL recombinant rat Fas Ligand.
Source
Mouse myeloma cell line, NS0-derived rat Fas/TNFRSF6/CD95 protein
>90%, by SDS-PAGE under reducing conditions and visualized by silver stain
Endotoxin Note
<0.10 EU per 1 μg of the protein by the LAL method.
Applications/Dilutions
Dilutions
Bioactivity
Theoretical MW
43.3 kDa (monomer). Disclaimer note: The observed molecular weight of the protein may vary from the listed predicted molecular weight due to post translational modifications, post translation cleavages, relative charges, and other experimental factors.
SDS-PAGE
60-65 kDa, reducing conditions
Publications
Read Publications using 2159-FA in the following applications:
Use a manual defrost freezer and avoid repeated freeze-thaw cycles.
12 months from date of receipt, -20 to -70 °C as supplied.
1 month, 2 to 8 °C under sterile conditions after reconstitution.
3 months, -20 to -70 °C under sterile conditions after reconstitution.
Buffer
Lyophilized from a 0.2 μm filtered solution in PBS.
Purity
>90%, by SDS-PAGE under reducing conditions and visualized by silver stain
Reconstitution Instructions
Reconstitute at 100 μg/mL in sterile PBS.
Notes
This product is produced by and ships from R&D Systems, Inc., a Bio-Techne brand.
Alternate Names for Recombinant Rat Fas/TNFRSF6/CD95 Fc Chimera Protein, CF
Apo-1 antigen
Apo-1
apoptosis antigen 1
Apoptosis-mediating surface antigen FAS
APT1
APT1FASTM
CD95 antigen
CD95
CD95ALPS1A
Fas (TNF receptor superfamily, member 6)
Fas AMA
Fas antigen
Fas
FAS1
FASLG receptor
TNFRSF6
TNFRSF6member 6
tumor necrosis factor receptor superfamily member 6
Background
Fas, also known as APO-1 or CD95, belongs to the death receptor subfamily of the TNF receptor superfamily and is designated TNFRSF6 (1 ‑ 3). Rat Fas cDNA encodes 324 amino acids (aa) that include a 21 aa signal peptide, a 150 aa extracellular domain (ECD) that contains three cysteine-rich TNFR repeats, a 17 aa transmembrane sequence, and a 136 aa cytoplasmic domain containing a death domain (DD), which is required for transducing apoptotic signals (4). Mature rat Fas ECD shares 68% aa sequence identity with mouse Fas, and 56 ‑ 58% with human, feline, bovine and porcine Fas. A 114 aa potential rat Fas isoform contains an alternate start site at aa 211, thus lacking all three TNFR repeats (5). The Fas ligand (FasL, TNFSF6) is a type II transmembrane protein of the TNF family that can be expressed on activated T-lymphocytes, NK cells and cells in immune privileged sites, or shed in soluble form (2). Engagement of FAS induces oligomerization of preformed Fas trimers (1, 2). The activated receptor recruits the adaptor molecule FADD to form the Death-Inducing Signaling Complex (DISC). Upon activation, caspases in the DISC initiate the apoptotic signaling cascade (6). Fas is prominent in epithelial cells, hepatocytes, activated mature lymphocytes, virus-transformed lymphocytes and tumor cells. It is an essential mediator in the activation-induced death of T lymphocytes that terminates the immune reaction (1, 2, 7). In immune-privileged tissues, infiltrating Fas-bearing lymphocytes and inflammatory cells are killed by FasL engagement (8). Both humans and mice with genetic defects in Fas accumulate abnormal lymphocytes and develop systemic autoimmunity (1 ‑ 3). The Fas pathway also appears to cross-communicate with the BIM (mitochondrial/intrinsic) apoptosis pathway (1).
Bouillet, P. and L.A. O’Reilly (2009) Nat. Rev. Immunol. 9:514.
Strasser, A. et al. (2009) Immunity 30:180.
Ashkenazi, A. and V. Dixit (1999) Curr. Opin. Cell Biol. 11:255.
SwissProt accession Q63199.
GenBank protein accession EDM13159.
Thorburn, A. (2003) Cellular Signaling 16:139.
Barreiro, R. et al. (2004) J. Immunol. 173:1519.
Ferguson, T.A. and T.S Griffith (2006) Immunol. Rev. 213:228.
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