Recombinant Human IL-17RE Fc Chimera Protein, CF Summary
| Details of Functionality |
Measured by its binding ability in a functional ELISA. When Recombinant Human IL-17 RE Fc Chimera is immobilized at 0.25 μg/mL (100 μL/well), the concentration of Recombinant Human IL-17C (Catalog # 1234-IL) that produces 50% of the optimal binding response is 1.5-7.5 ng/mL. |
| Source |
Chinese Hamster Ovary cell line, CHO-derived human IL-17 RE protein
Human IL-17 RE (Thr155-His454) Accession # Q8NFR9 |
IEGRMD |
Human IgG1 (Pro100-Lys330) |
| N-terminus |
|
C-terminus |
|
|
| Accession # |
|
| N-terminal Sequence |
Thr155 |
| Structure / Form |
Disulfide-linked homodimer |
| Protein/Peptide Type |
Recombinant Proteins |
| Gene |
IL17RE |
| Purity |
>90%, by SDS-PAGE with silver staining |
| Endotoxin Note |
<0.10 EU per 1 μg of the protein by the LAL method. |
Applications/Dilutions
| Dilutions |
|
| Theoretical MW |
61 kDa (monomer). 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 |
62-75 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 with silver staining |
| Reconstitution Instructions |
Reconstitute at 100 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 IL-17RE Fc Chimera Protein, CF
Background
Interleukin-17 Receptor E (IL-17 RE) is an approximately 70 kDa (predicted) transmembrane protein in the family of IL-17 receptors. IL-17 RE is required for mediating the pro-inflammatory and homeostatic actions of IL-17C in the skin and mucosa (1, 2). Mature human IL-17 RE consists of a 431 amino acid (aa) extracellular domain, a 21 aa transmembrane segment, and a 192 aa cytoplasmic domain with one SEFIR/TIR domain (3). Within aa 115-454, human IL-17 RE shares 79% aa sequence identity with mouse and rat IL-17 RE. Alternative splicing of human IL-17 RE generates additional isoforms with a 116 aa N-terminal deletion and/or substitution and truncation in the ECD following aa 268 or aa 433. IL-17 RE is expressed on keratinocytes, mucosal epithelial cells, Th17 cells, and gamma /δ T cells (4, 5). It associates with the widely expressed IL-17 RA to form a heterodimeric receptor for IL-17C (4-6). IL-17C binds to IL-17 RE with high affinity and to IL-17 RA with low affinity (4, 5). IL-17C expression is induced by inflammatory stimulation in colon and airway epithelial cells, keratinocytes, CD4
+ T cells, macrophages, and dendritic cells (4, 6, 7-9). It is up-regulated in various chronic inflammatory diseases including psoriasis, cystic fibrosis, and chronic obstructive pulmonary disease (COPD) (7, 8, 10). IL-17 RE is reciprocally down-regulated in psoriatic lesions (10). The interaction of IL-17C with IL-17 RE promotes mucosal immunity through the induction of anti-bacterial peptides and pro-inflammatory cytokines and chemokines (4, 6, 8, 9). IL-17C action supports the integrity of the colon epithelium following infection induced damage (4, 6, 11) but also contributes to psoriatic skin thickening and the progression of arthritis (4, 8, 9). IL-17C is additionally up-regulated in Th17 cell dependent autoimmunity (5). In this setting, it exacerbates disease severity by inducing Th17 cell production of IL-17A, IL-17F, IL-22, CCR6, and CCL20 (5). The up-regulation of IL-17 RE in hepatocellular carcinoma is associated with poor prognosis (12).
- Pappu, R. et al. (2012) Trends Immunol. 33:343.
- Rubino, S.J. et al. (2012) Trends Immunol. 33:112.
- Li, T.S. et al. (2006) Cell. Signal. 18:1287.
- Ramirez-Carrozzi, V. et al. (2011) Nat. Immunol. 12:1159.
- Chang, S.H. et al. (2011) Immunity 35:611.
- Song, X. et al. (2011) Nat. Immunol. 12:1151.
- Pfeifer, P. et al. (2013) Am. J. Respir. Cell Mol. Biol. 48:415.
- Johnston, A. et al. (2013) J. Immunol. 190:2252.
- Yamaguchi, Y. et al. (2007) J. Immunol. 179:7128.
- Johansen, C. et al. (2009) Br. J. Dermatol. 160:319.
- Reynolds, J.M. et al. (2012) J. Immunol. 189:4226.
- Liao, R. et al. (2013) J. Exp. Clin. Cancer Res. 32:3.
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