Recombinant Mouse GITR Ligand/TNFSF18 (aa 47-173) Protein Summary
Details of Functionality
Measured by its ability to stimulate mouse T cell proliferation in the presence of anti-CD3. The ED50 for this effect is 0.02‑0.3 µg/mL in the presence of 10 µg/mL of a cross-linking antibody, Mouse Anti-polyHistidine Monoclonal Antibody (Catalog # MAB050).
Source
Mouse myeloma cell line, NS0-derived mouse GITR Ligand/TNFSF18 protein Thr47-Ser173, with an N-terminal 10-His tag
>95%, 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
16 kDa. 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
16-26 kDa, reducing conditions
Publications
Read Publications using 2177-GL 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 with BSA as a carrier protein.
Purity
>95%, by SDS-PAGE under reducing conditions and visualized by silver stain
Reconstitution Instructions
Reconstitute at 100 μg/mL in sterile PBS containing at least 0.1% human or bovine serum albumin.
Notes
This product is produced by and ships from R&D Systems, Inc., a Bio-Techne brand.
Alternate Names for Recombinant Mouse GITR Ligand/TNFSF18 (aa 47-173) Protein
Activation-inducible TNF-related ligand
AITRL
AITRLMGC138237
GITR Ligand
GITRL
GITRLglucocorticoid-induced TNFR-related protein ligand
Glucocorticoid-induced TNF-related ligand
hGITRLGITR ligand
TL6AITR ligand
TNFSF18
tumor necrosis factor (ligand) superfamily, member 18
tumor necrosis factor ligand superfamily member 18
Background
GITR Ligand, also known as TNFSF18 and TL6, is an approximately 30 kDa type II transmembrane glycoprotein in the TNF superfamily (1). Mouse GITR Ligand consists of a 23 amino acid (aa) cytoplasmic domain, a 19 aa transmembrane segment, and a 131 aa extracellular domain (ECD) (2 ‑ 4). Within the ECD, mouse GITR Ligand shares 56% and 81% aa sequence identity with human and rat GITR Ligand, respectively. GITR Ligand is expressed on antigen presenting cells, CD4-CD8- double negative thymic precursors, vascular endothelial cells, neurons, and in the eye (4 ‑ 11). Its expression is transiently up‑regulated by proinflammatory stimulation (5, 8, 11). The binding of GITR Ligand to GITR on mouse CD25+ Treg cells permits the reactivation of T cells from Treg‑induced suppression, although this does not appear to occur in humans (9, 12 ‑ 14). GITR Ligand binding to GITR additionally provides a costimulatory signal to activated CD4+ and CD8+ T cells and NK cells (6, 15, 16). This interaction also induces reverse signaling in GITR Ligand expressing dendritic cells to suppress cellular activation through the same pathway induced by the immunosuppressant dexamethasone (17). In the brain, GITR Ligand/GITR interactions enhance NGF‑mediated neurite outgrowth from sympathetic neurons (10).
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Yu, K.Y. et al. (2003) Biochem. Biophys. Res. Commun. 310:433.
Kim, J.D. et al. (2003) Genes Immun. 4:564.
Tone, M. et al. (2003) Proc. Natl. Acad. Sci. 100:15059.
Stephens, G.L. et al. (2004) J. Immunol. 173:5008.
Hanabuchi, S. et al. (2006) Blood 107:3617.
Kamimura, Y. et al. (2009) J. Immunol. 182:2708.
Hwang, H. et al. (2010) J. Neurosci. Res. 88:2188.
Tuyaerts, S. et al. (2007) J. Leukoc. Biol. 82:93.
O’Keefe, G.W. et al. (2008) Nat. Neurosci. 11:135.
Kim, B.J. et al. (2004) Invest. Ophthalmol. Vis. Sci. 45:3170.
Shimizu, J. et al. (2002) Nat. Immunol. 3:135.
Ji, H. et al. (2004) J. Immunol. 172:5823.
McHugh, R.S. et al. (2002) Immunity 16:311.
Kanamaru, F. et al. (2004) J. Immunol. 172:7306.
Ronchetti, S. et al. (2004) Eur. J. Immunol. 34:613.
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