Recombinant Rat GITR Ligand/TNFSF18 Protein, CF

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Recombinant Rat GITR Ligand/TNFSF18 (Catalog # 9735-GL)induces IL-8 secretion in HT1080 human fibrosarcoma cells transfected with ratGITR. The ED50 for this effect is 0.06-0.6 µg/mL.

Product Details

Summary
Reactivity RtSpecies Glossary
Applications Bioactivity
Format
Carrier-Free

Order Details

Recombinant Rat GITR Ligand/TNFSF18 Protein, CF Summary

Details of Functionality
Measured by its ability to induce IL-8 secretion in HT1080 human fibrosarcoma cells transfected with rat GITR. The ED50 for this effect is 0.06-0.6 μg/mL in the presence of Mouse Anti-Hemagglutinin/HA Peptide Monoclonal Antibody (Catalog # MAB060).
Source
Mouse myeloma cell line, NS0-derived rat GITR Ligand/TNFSF18 protein
Thr74-Ser200, with a N-terminal HA-tag
Accession #
N-terminal Sequence
Tyr
Protein/Peptide Type
Recombinant Proteins
Purity
>85%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining.
Endotoxin Note
<0.10 EU per 1 μg of the protein by the LAL method.

Applications/Dilutions

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
19-22 kDa, reducing conditions

Packaging, Storage & Formulations

Storage
  • 12 months from date of receipt, ≤ -20 °C as supplied.
  • 1 month, 2 to 8 °C under sterile conditions after reconstitution.
  • 3 months, ≤ -20 °C under sterile conditions after reconstitution.
Buffer
Lyophilized from a 0.2 μm filtered solution in PBS.
Purity
>85%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining.
Reconstitution Instructions
Reconstitute at 500 μg/mL in PBS.

Notes

This product is produced by and ships from R&D Systems, Inc., a Bio-Techne brand.

Alternate Names for Recombinant Rat GITR Ligand/TNFSF18 Protein, CF

  • 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). Rat GITR Ligand consists of a 20 amino acid (aa) cytoplasmic domain, a 21 aa transmembrane segment, and a 132 aa extracellular domain (ECD) (2-4). Within the ECD, rat GITR Ligand shares 60.6% and 81.1% aa sequence identity with human and mouse 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+ T reg 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 co-stimulatory 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).
  1. Azuma, M. (2010) Crit. Rev. Immunol. 30:547.
  2. Yu, K.Y. et al. (2003) Biochem. Biophys. Res. Commun. 310:433.
  3. Kim, J.D. et al. (2003) Genes Immun. 4:564.
  4. Tone, M. et al. (2003) Proc. Natl. Acad. Sci. 100:15059.
  5. Stephens, G.L. et al. (2004) J. Immunol. 173:5008.
  6. Hanabuchi, S. et al. (2006) Blood 107:3617.
  7. Kamimura, Y. et al. (2009) J. Immunol. 182:2708.
  8. Hwang, H. et al. (2010) J. Neurosci. Res. 88:2188.
  9. Tuyaerts, S. et al. (2007) J. Leukoc. Biol. 82:93.
  10. O'Keefe, G.W. et al. (2008) Nat. Neurosci. 11:135.
  11. Kim, B.J. et al. (2004) Invest. Ophthalmol. Vis. Sci. 45:3170.
  12. Shimizu, J. et al. (2002) Nat. Immunol. 3:135.
  13. Ji, H. et al. (2004) J. Immunol. 172:5823.
  14. McHugh, R.S. et al. (2002) Immunity 16:311.
  15. Kanamaru, F. et al. (2004) J. Immunol. 172:7306.
  16. Ronchetti, S. et al. (2004) Eur. J. Immunol. 34:613.
  17. Grohmann, U. et al. (2007) Nat. Med. 13:579.

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