Recombinant Rat GITR/TNFRSF18 Fc Chimera Protein, CF

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When Recombinant Rat GITR/TNFRSF18 Fc Chimera isimmobilized at 2 μg/mL,Recombinant Mouse GITR Ligand/TNFSF18 aa 47-173 (Catalog # 2177-GL) bindswith an ED50 of 25-150 ng/mL.

Product Details

Summary
Reactivity RtSpecies Glossary
Applications Bioactivity
Format
Carrier-Free

Order Details

Recombinant Rat GITR/TNFRSF18 Fc Chimera Protein, CF Summary

Details of Functionality
Measured by its binding ability in a functional ELISA. When Recombinant Rat GITR/TNFRSF18 Fc Chimera is immobilized at 2 μg/mL, 100 μL/well, the concentration of Recombinant Mouse GITR Ligand/TNFSF18 aa 47-173 (Catalog # 2177-GL) that produces 50% of the optimal binding response is 25-150 ng/mL
Source
Mouse myeloma cell line, NS0-derived rat GITR/TNFRSF18 protein
Rat GITR/TNFRSF18
(Glu25-His153)
Accession # NP_001019520
IEGRMDP Mouse IgG2a
(Glu98-Lys330)
N-terminus C-terminus
Accession #
N-terminal Sequence
Glu25
Structure / Form
Disulfide-linked homodimer
Protein/Peptide Type
Recombinant Proteins
Purity
>90%, 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
41 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
55-64 kDa, reducing conditions

Packaging, Storage & Formulations

Storage
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 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/TNFRSF18 Fc Chimera Protein, CF

  • Activation-inducible TNFR family receptor
  • AITR
  • AITRTNF receptor superfamily activation-inducible protein
  • CD357 antigen
  • CD357
  • GITR
  • GITR-D
  • GITRtumor necrosis factor receptor superfamily member 18
  • Glucocorticoid-induced TNFR-related protein
  • TNFRSF18
  • tumor necrosis factor receptor superfamily, member 18

Background

GITR (glucocorticoid-induced tumor necrosis factor receptor), also known as AITR and TNFRSF18, is a 40 kDa transmembrane glycoprotein that functions in immune regulation (1, 2). Mature rat GITR consists of a 134 amino acid (aa) extracellular domain (ECD) with three tandem TNFR cysteine-rich repeats, a 21 aa transmembrane segment, and a 55 aa cytoplasmic domain. Within the ECD, rat GITR shares 60% and 86% aa sequence identity with human and mouse GITR, respectively. Alternative splicing generates additional isoforms with an N-terminal extension or a substitution in the cytoplasmic domain. GITR is expressed on CD4+CD25+ regulatory T cells (Treg) as well as on subsets of thymocytes, lymph node cells, and splenocytes (3-5), and it is up-regulated on antigen-activated conventional CD4+ and CD8+ T cells (4-7). GITR binding by GITR Ligand/TNFSF18 costimulates the proliferation and activation of CD4+ or CD8+ conventional T cells (6-9). It also induces the proliferation of Treg (8, 10) but inhibits the ability of Treg to suppress immune responses (3, 8, 11-13). This can result in the development of autoimmunity, increased tumor cell killing by effector T cells (3, 11), and increased inflammation in arthritis, allergic asthma, and inflammatory bowel disease (10, 14). GITR is also expressed on sympathetic neurons where it enhances NGF-induced neurite outgrowth and branching (15).
  1. Clouthier, D.L. and T.H. Watts (2014) Cytokine Growth Factor Rev. 25:91.
  2. Ronchetti, S. et al. (2015) J. Immunol. Res. 2015:171520.
  3. Shimizu, J. et al. (2002) Nat. Immunol. 3:135.
  4. Nocentini, G. et al. (1997) Proc. Natl. Acad. Sci. USA 94:6216.
  5. Kwon, B. et al. (1999) J. Biol. Chem. 274:6056.
  6. Gurney, A.L. et al. (1999) Curr. Biol. 9:215.
  7. Muriglan, S.J. et al. (2004) J. Exp. Med. 200:149.
  8. Ronchetti, S. et al. (2004) Eur. J. Immunol. 34:613.
  9. Tone, M. et al. (2003) Proc. Natl. Acad. Sci. USA 100:15059.
  10. Ephrem, A. et al. (2013) Eur. J. Immunol. 43:2421.
  11. Ko, K. et al. (2005) J. Exp. Med. 202:885.
  12. Ji, H. et al. (2004) J. Immunol. 172:5823.
  13. Stephens, G.L. et al. (2004) J. Immunol. 173:5008.
  14. Patel, M. et al. (2005) Eur. J. Immunol. 35:3581.
  15. O'Keeffe, G.W. et al. (2008) Nat. Neurosci. 11:135.

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