Recombinant Human IL-27 Ra/WSX-1/TCCR Avi His Protein, CF

When Recombinant Human IL-27 Protein (2526-IL/CF) is immobilized at 4 µg/mL (100 µL/well), Biotinylated Recombinant Human IL-27 R alpha /WSX-1/TCCR Avi-tag His-tag Protein (Catalog # AVI11270) binds with an ED50 of 30.0-360 ng/mL.

2 μg/lane of Recombinant Human IL-27 Ra/WSX-1/TCCR Avi-tag His-tag Protein (Catalog # AVI11270) was resolved with SDS-PAGE under reducing (R) and non-reducing (NR) conditions and visualized by Coomassie® Blue staining, showing bands at 81-92 kDa.

• Applications: Bioactivity
• Format: Carrier-Free

Recombinant Human IL-27 Ra/WSX-1/TCCR Avi His Protein, CF Summary

• Additional Information: Biotinylated
• Details of Functionality: Measured by its binding ability in a functional ELISA. When Recombinant Human IL-27 (Catalog # 2526-IL/CF) is immobilized at 4 µg/mL (100 µL/well), Biotinylated Recombinant Human IL-27 R alpha /WSX-1/TCCR Avi-tag His-tag (Catalog # AVI11270) binds with an ED₅₀ of 30.0-360 ng/mL.
• Source: Chinese Hamster Ovary cell line, CHO-derived human IL-27 R alpha/WSX-1/TCCR protein
  

  Human IL-27 R alpha /WSX-1/TCCR (Gln33-Lys516) Accession # Q6UWB1.2	Avi-tag	6-His tag
  N-terminus		C-terminus

• Accession #: Q6UWB1.2
• N-terminal Sequence: Gln33; deduced from Gly34 after deblocking
• Structure / Form: 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: 57 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: 81-92 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 250 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-27 Ra/WSX-1/TCCR Avi His 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). Our Avi-tag Biotinylated human IL-27 R alpha features biotinylation at a single site contained within the Avi-tag, a unique 15 amino acid peptide. Protein orientation will be uniform when bound to streptavidin-coated surface due to the precise control of biotinylation and the rest of the protein is unchanged so there is no interference in the protein's bioactivity.

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.

Bioinformatics

• Uniprot:
  • Q6UWB1.2()