Recombinant Cynomolgus Monkey GITR/TNFRSF18 Fc Chimera, CF Summary
Details of Functionality |
Measured by its binding ability in a functional ELISA. When Recombinant Cynomolgus Monkey GITR/TNFRSF18 Fc Chimera
is immobilized at 0.5 μg/mL, 100 μL/well, the concentration of biotinylated recombinant human GITR Ligand/TNFSF18 that produces 50% of the optimal binding
response is 8-40 ng/mL. |
Source |
Chinese Hamster Ovary cell line, CHO-derived cynomolgus monkey GITR/TNFRSF18 protein Cynomolgus Monkey GITR/TNFRSF18 (Gln20-Glu155) Accession # XP_005545180 | IEGRMD | Human IgG1 (Pro100-Lys330) | N-terminus | | C-terminus | |
|
Accession # |
|
N-terminal Sequence |
No results obtained. Gln20 inferred from enzymatic pyroglutamate treatment revealing Arg21 |
Structure / Form |
Disulfide-linked homodimer |
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 |
|
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 |
49-60 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 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 Cynomolgus Monkey GITR/TNFRSF18 Fc Chimera, CF
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
TNF R cysteine-rich repeats, a 21 aa transmembrane segment, and a 58 aa
cytoplasmic domain (3, 4). Within the ECD region, cyno GITR shares 89.8% and
53.2% aa sequence identity with human and mouse 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 TNF R
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
up-regulated on antigen-activated conventional CD4
+ and CD8
+
T cells (3, 4, 6, 7). GITR binding by GITR Ligand/TNFSF18 co-stimulates 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).
- Clouthier, D.L. and T.H. Watts (2014) Cytokine Growth Factor Rev. 25:91.
- Ronchetti, S. et al. (2015) J. Immunol. Res. 2015:171520.
- Gurney, A.L. et al. (1999) Curr. Biol. 9:215.
- Kwon, B. et al. (1999) J. Biol. Chem. 274:6056.
- Shimizu, J. et al. (2002) Nat. Immunol. 3:135.
- Nocentini, G. et al. (1997) Proc. Natl. Acad. Sci. USA 94:6216.
- Muriglan, S.J. et al. (2004) J. Exp. Med. 200:149.
- Ronchetti, S. et al. (2004) Eur. J. Immunol. 34:613.
- Tone, M. et al. (2003) Proc. Natl. Acad. Sci. USA 100:15059.
- Ephrem, A. et al. (2013) Eur. J. Immunol. 43:2421.
- Ko, K. et al. (2005) J. Exp. Med. 202:885.
- Ji, H. et al. (2004) J. Immunol. 172:5823.
- Stephens, G.L. et al. (2004) J. Immunol. 173:5008.
- Patel, M. et al. (2005) Eur. J. Immunol. 35:3581.
- O'Keeffe, G.W. et al. (2008) Nat. Neurosci. 11:135.
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