Recombinant Cynomolgus Monkey IL-17RA/IL-17R His Protein, CF Summary
| Additional Information |
His-tag, Analyzed by SEC-MALS |
| Details of Functionality |
Measured by its ability to inhibit IL-17-induced IL-6 secretion by NIH‑3T3 mouse embryonic fibroblast cells. The ED 50 for this effect is 0.010‑0.100 µg/mL in the presence of 10.0 ng/mL Recombinant Human IL‑17 (Catalog #
7955-IL). |
| Source |
Chinese Hamster Ovary cell line, CHO-derived cynomolgus monkey IL-17RA/IL-17R protein Leu33-Trp320, with a C-terminal 6-His tag |
| Accession # |
|
| N-terminal Sequence |
Leu33 |
| 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 |
34 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 |
59-67 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 Cynomolgus Monkey IL-17RA/IL-17R His Protein, CF
Background
IL-17 R, also known as IL-17 RA, is a 120 kDa type I transmembrane glycoprotein protein that plays a central role in inflammatory responses (1-3). Mature mouse IL‑17 R consists of a 291 amino acid (aa) extracellular domain, a 21 aa transmembrane segment, and a 521 aa cytoplasmic domain (4). The cytoplasmic domain contains a region homologous to the TIR domain of the TLR/IL-1 R family (5). Within the extracellular domain, cynomolgus monkey IL-17RA shares 95% sequence identity with human IL-17RA. While the expression of IL-17 is restricted to activated T cells, IL-17 R exhibits a broad tissue distribution (4). Even in the absence of ligand, IL-17 R exists on the cell surface as a multimer (6). IL-17 R can bind IL-17 but must associate with IL-17 RC to transduce signals (7, 8). Interestingly, human IL-17 R does not appear to form productive complexes with mouse IL-17 RC (8). The IL-17 R can also signal in response to IL-17F (9). IL-17 R ligation promotes T cell activation and the production of IL-6, G-CSF, SCF, and multiple pro‑inflammatory chemokines (4, 7, 9, 10). IL-17A and IL-17F synergize with TNF-alpha in the induction of CXCL1, G-CSF, and IL-6 (9, 11). This effect requires the presence of both TNF RI and TNF RII (9). IL-17 interactions with IL-17 R also inhibit the TNF-alpha induced up-regulation of fibroblast CCL5 and VCAM-1 (11). CCL5 and VCAM-1 induced effects are differentially sensitive to blockade with IL-17 R specific antibodies, suggesting that IL-17 R triggers divergent intracellular signals (11).
In vivo, IL‑17 R activity is important for increased generation of neutrophils and their recruitment to sites of inflammation (10, 12, 13). IL-17 R is required for host defense against microbial infection and for the progression of arthritis from inflammation to destructive joint erosion (10, 13).
- Iwakura, Y. and H. Ishigame (2006) J. Clin. Invest. 116:1218.
- Moseley, T.A. et al. (2003) Cytokine Growth Factor Rev. 14:155.
- Kawaguchi, M. et al. (2004) J. Allergy Clin. Immunol. 114:1265.
- Yao, Z. et al. (1995) Immunity 3:811.
- Novatchkova, M. et al. (2003) Trends Biochem. Sci. 28:226.
- Kramer, J.M. et al. (2006) J. Immunol. 176:711.
- Hymowitz, S.G. et al. (2001) EMBO J. 20:5332.
- Toy, D. et al. (2006) J. Immunol. 177:36.
- McAllister, F. et al. (2005) J. Immunol. 175:404.
- Ye, P. et al. (2001) J. Exp. Med. 194:519.
- Schnyder, B. et al. (2005) Cytokine 31:191.
- Tan, W. et al. (2006) J. Immunol. 176:6186.
- Lubberts, E. et al. (2005) J. Immunol. 175:3360.
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