Recombinant Human GITR/TNFRSF18 Fc Avi-tag Protein, CF

When Recombinant Human GITR Ligand/TNFSF18 (Catalog # 6987-GL) is immobilized at 0.5 μg/mL, 100 μL/well, Biotinylated Recombinant Human GITR/TNFRSF18 Fc Chimera Avi-tag (Catalog # AVI689) binds with an ED50 of 0.05-0.5 μg/mL.

2 μg/lane of Biotinylated Recombinant Human GITR/TNFRSF18 Fc Chimera Avi-tag (Catalog # AVI689) was resolved with SDS-PAGE under reducing (R) and non-reducing (NR) conditions and visualized by Coomassie® Blue staining, showing bands at 54-60 kDa and 108-120 kDa.

• Reactivity: Hu
• Applications: Bioactivity
• Format: Carrier-Free

Recombinant Human GITR/TNFRSF18 Fc Avi-tag Protein, CF Summary

• Additional Information: Biotinylated
• Details of Functionality: Measured by its binding ability in a functional ELISA. When Recombinant Human GITR Ligand/TNFSF18 (Catalog # 6987-GL) is immobilized at 0.5 μg/mL (100 μL/well), It binds to Biotinylated Recombinant Human GITR/TNFRSF18 Fc Chimera Avi-tag (Catalog # AVI689) with an ED₅₀ of 0.05-0.5 μg/mL.
• Source: Chinese Hamster Ovary cell line, CHO-derived human GITR/TNFRSF18 protein
  

  GITR/TNFRSF18 (Gln26-Glu161) Accession # Q9Y5U5.1	IEGRMD	Human IgG1 (Pro100-Lys330)	Avi-tag

• Accession #: Q9Y5U5.1
• N-terminal Sequence: Gln26 inferred from enzymatic pyroglutamate treatment revealing Arg27
• Structure / Form: Disulfide-linked homodimer, biotinylated via Avi-tag
• Protein/Peptide Type: Recombinant Proteins
• Purity: >95%, 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

• Dilutions:
  • Bioactivity
• Theoretical MW: 43 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: 54-60 kDa, under 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 with Trehalose.
• Purity: >95%, 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 Human GITR/TNFRSF18 Fc Avi-tag 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 human GITR consists of a 137 amino acid (aa) extracellular domain (ECD) with three tandem TNFR cysteine-rich repeats, a 21 aa transmembrane segment, and a 58 aa cytoplasmic domain (3, 4). Within the ECD, human GITR shares 55% and 60% aa sequence identity with mouse and rat GITR, respectively. Alternative splicing generates an isoform with a short deletion in the cytoplasmic domain and a potentially secreted isoform that is substituted within the third TNFR repeat and lacks the transmembrane and cytoplasmic regions. GITR is expressed on CD4⁺CD25⁺ regulatory T cells (Treg) as well as on subsets of thymocytes, lymph node cells, and splenocytes (4-6), and it is upregulated on antigen-activated conventional CD4⁺ and CD8⁺ T cells (3, 4, 6, 7). GITR binding by GITR Ligand/TNFSF18 costimulates the proliferation and activation of CD4⁺ or CD8⁺ conventional T cells (3, 7-9). It also induces the proliferation of Treg (8, 10) but inhibits the ability of Treg to suppress immune responses (5, 8, 11-13). This can result in the development of autoimmunity, increased tumor cell killing by effector T cells (5, 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. Gurney, A.L. et al. (1999) Curr. Biol. 9:215.
4. Kwon, B. et al. (1999) J. Biol. Chem. 274:6056.
5. Shimizu, J. et al. (2002) Nat. Immunol. 3:135.
6. Nocentini, G. et al. (1997) Proc. Natl. Acad. Sci. USA 94:6216.
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.

Bioinformatics

• Uniprot:
  • Q9Y5U5.1()