Recombinant Human IL-27 Ra/WSX-1/TCCR Fc Chimera Protein, CF

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Product Details

Summary
Reactivity HuSpecies Glossary
Applications Bioactivity
Format
Carrier-Free

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Recombinant Human IL-27 Ra/WSX-1/TCCR Fc Chimera Protein, CF Summary

Details of Functionality
Measured by its ability to inhibit IL-27 anti-viral activity using HepG2 human hepatocellular carcinoma cells infected with encephalomyocarditis (EMC) virus. Bender H. et al. (2009) Hepatology 50:585. The ED50 for this effect is 0.75‑4.5 µg/mL.
Source
Mouse myeloma cell line, NS0-derived human IL-27 R alpha/WSX-1/TCCR protein
Human IL-27 R alpha
(Gly34-Lys516)
Accession # Q6UWB1
IEGRMD Human IgG1
(Pro100-Lys330)
N-terminus C-terminus
Accession #
N-terminal Sequence
Gly34
Structure / Form
Disulfide-linked homodimer
Protein/Peptide Type
Recombinant Proteins
Gene
IL27RA
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

Dilutions
  • Bioactivity
Theoretical MW
79 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
100-110 kDa, reducing conditions
Publications
Read Publications using
1479-TC in the following applications:

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 100 μg/mL in sterile PBS.

Notes

This product is produced by and ships from R&D Systems, Inc., a Bio-Techne brand.

Alternate Names for Recombinant Human IL-27 Ra/WSX-1/TCCR Fc Chimera Protein, CF

  • class I cytokine receptor
  • CRL1IL-27R
  • Cytokine receptor-like 1
  • IL-27 R alpha
  • IL27R alpha
  • IL27R
  • IL27RA
  • IL-27Ra
  • IL-27R-alpha
  • interleukin 27 receptor, alpha
  • interleukin-27 receptor subunit alpha
  • TCCR
  • TCCRIL-27 receptor subunit alpha
  • T-cell cytokine receptor type 1
  • Type I T-cell cytokine receptor
  • WSX-1
  • WSX1IL-27R subunit alpha
  • zcytor1

Background

IL‑27 R alpha (also known as WSX‑1 and TCCR) is a 96 ‑ 100 kDa member of the type I, group 2 cytokine receptor family (1, 2, 3, 4, 5, 6). Mature IL‑27 R alpha  is a type I transmembrane glycoprotein that contains a 484 amino acid (aa) extracellular region, a 21 aa transmembrane segment and a 99 aa cytoplasmic domain. Consistent with type I cytokine receptors, the extracellular region contains four positionally conserved cysteine residues, a WSxWS motif (for receptor folding and ligand binding), and three fibronectin type III repeats. The intracellular domain contains a "box‑1" motif that may be involved with Janus kinases (3). One potential alternate splice form has been hypothesized that involves a 58 aa addition to the cytoplasmic domain and, based on mouse, a soluble 33 kDa splice form that shows a 20 aa substitution for aa 257 ‑ 636 may also occur in human (3, 7). The human IL‑27 R alpha extracellular region shares 63% amino acid identity with the mouse IL‑27 R alpha extracellular domain (2, 3). IL‑27 R alpha is expressed in mast cells, endothelial cells, NK cells, macrophages, monocytes, B cells, dendritic cells, and naïve T cells (1, 2, 4, 8). Typical of other class I cytokine receptor chains, the ligand binding IL‑27 R alpha molecule is known to heterodimerize with a signal‑transducing subunit (gp130) to form a functional IL‑27 receptor (9, 10). In addition, IL‑27 R alpha is reported to complex with CNTFR alpha and gp130 form a humanin receptor on neurons (7, 11), and to complex with gp130 and IL‑6 R to form a receptor for a p28:CLF heterodimeric cytokine on lymphocytes (12). Studies using IL‑27 R alpha /WSX‑1‑/‑ mice reveal that IL‑27 has the ability to suppress T cell activity during infection, and to mediate an inhibition of both type 1 and type 2 T cell immunity (4, 13, 14). In particular, IL‑27 is known to act on naïve T cells, blocking their differentiation into a Th17 phenotype. Notably, cells committed to a Th17 phenotype, although they express a functional IL‑27 receptor, are unresponsive to the effects of IL‑27 (15). Activated T cells that are CD4+ and CD8+, and which express the IL‑27 receptor, can be induced by
IL‑27 to form a double‑positive CD25+ FoxP3 IFN‑ gamma plus IL‑10 secreting phenotype that both promotes and suppresses the inflammatory response (16).

  1. Villarino, A.V. et al. (2004) J. Immunol. 173:715.
  2. Chen, Q. et al. (2000) Nature 407:916.
  3. Sprecher, C.A. et al. (1998) Biochem. Biophys. Res. Commun. 246:82.
  4. Artis, D. et al. (2004) J. Immunol. 173:5626.
  5. Yoshida, H. & Y. Miyazaki (2008) Int. J. Biochem. Cell Biol. 40:2379.
  6. Yoshida, H. & M. Yoshiyuki (2008) Immunol. Rev. 226:234.
  7. Hashimoto, Y. et al. (2009) Biochem. Biophys. Res. Commun. 389:95.
  8. Holscher, C. et al. (2005) J. Immunol. 174:3534.
  9. Pflanz, S. et al. (2004) J. Immunol. 172:2225.
  10. Scheller, J. et al. (2005) Biochem. Biophys. Res. Commun. 326:724.
  11. Hashimoto, Y. et al. (2009) Mol. Biol. Cell 20:2864.
  12. Crabe, S. et al. (2009) J. Immunol. 183:7692.
  13. Villarino, A. et al. (2003) J. Immunol. 170:645.
  14. Hamano., S. et al. (2003) Immunity 19:657.
  15. El-behi, M. et al. (2009) J. Immunol. 183:4957.
  16. Fitzgerald, D.C. et al. (2007) Nat. Immunol. 8:1372.

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Bioinformatics

Gene Symbol IL27RA
Uniprot