Recombinant Human IL-10 R beta Fc Chimera Protein, CF

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Recombinant Human IL-10 R beta Fc Chimera Protein (Catalog # 11460-RB) binds Recombinant Human IL-28 R alpha /IFN-lambda R1 Fc Chimera (5260-MR) in the presence of Recombinant Human IL-28B/IFN-lambda 3 (5259-IL/CF) ...read more
2 μg/lane of Recombinant Human IL‑10 R beta Fc Chimera Protein (Catalog # 11460-RB) was resolved with SDS-PAGE under reducing (R) and non-reducing (NR) conditions and visualized by Coomassie® Blue staining, ...read more

Product Details

Summary
Reactivity HuSpecies Glossary
Applications Bioactivity
Format
Carrier-Free

Order Details

Recombinant Human IL-10 R beta Fc Chimera Protein, CF Summary

Additional Information
CHO expressed
Details of Functionality
Measured by its binding ability in a functional ELISA. Recombinant Human IL-10 R beta Fc Chimera (Catalog # 11460-RB) binds Recombinant Human IL-28 R alpha /IFN-lambda R1 Fc Chimera (Catalog # 5260-MR) in the presence of Recombinant Human IL-28B/IFN-lambda 3 (Catalog # 5259-IL/CF) with an ED50 of 0.250-3.00 µg/mL.
Source
Chinese Hamster Ovary cell line, CHO-derived human IL-10 R beta protein
Human IL-10 R beta
(Met20-Ser220)
Accession # Q08334.2
GGIEGRMD Human IgG1
(Pro100-Lys330)
N-terminusC-terminus
Accession #
N-terminal Sequence
Met20
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
  • Bioactivity
Theoretical MW
50 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
72-82 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.
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 Human IL-10 R beta Fc Chimera Protein, CF

  • CDw210b antigen
  • CDw210b
  • CRF2-4IL-10R subunit 2
  • CRFB4
  • CRFB4human transmembrane receptor protein; cytokine receptor10CDW210B
  • D21S58
  • D21S66
  • IBD25
  • IL-10 R beta
  • IL-10 receptor subunit beta
  • IL10R beta
  • IL-10R2
  • IL-10R2IL-10R subunit beta
  • IL10RB
  • IL-10Rb
  • interleukin 10 receptor, beta
  • Interleukin-10 receptor subunit 2
  • interleukin-10 receptor subunit beta
  • member 4

Background

Interleukin-10 Receptor beta (IL-10 R beta ), also known as IL-10 R2 and CRF2-4, is a 60 kDa transmembrane glycoprotein that functions as a co-receptor for several class 2 cytokines including Interleukins-10, -22, -26, -28A/IFN-lambda 2, -28B/IFN-lambda 3, and -29/IFN-lambda (1, 2). IL-10 R beta associates with ligand‑specific receptor subunits to form signaling receptor complexes, e.g. IL-10 R alpha for IL-10 (3, 4), IL-20 R alpha for IL-26 (5, 6), IL-22 R alpha for IL-22 (7, 8), and IL-28 R alpha for IL-28A, IL-28B, and IL-29 (9, 10). IL‑10 R beta is widely expressed, while the associated receptor subunits exhibit differential expression patterns (1). The ligand‑specific subunits are responsible for the divergent functions of these cytokines, encompassing immune suppression, promotion or inhibition of inflammation, mucosal defense, antiviral immunity, and hematopoiesis (1). IL-10 R beta deficient mice lack responsiveness to each of those cytokines. IL-10 R beta contributes to ligand binding, but effective signaling is only triggered in the presence of the ligand‑specific subunit (8, 9, 11). In the case of IL-10, a cytokine dimer binds to two IL‑10 R alpha /IL-10R1 chains, resulting in recruitment of two IL-10 R beta /IL-10R2 chains (3, 12). Some members of the IL-10 family are monomeric cytokines and interact with single molecules of IL-10 R beta and their ligand‑specific subunit (1). Mature human IL-10 R beta consists of a 201 amino acid (aa) extracellular region with two fibronectin type-III domains, a 22 aa transmembrane segment and a 83 aa cytoplasmic domain (13). Within the ECD, human IL-10 R beta shares 75% and 78% aa sequence identity with mouse and rat IL-10 R beta , respectively.
  1. Commins, S. et al. (2008) J. Allergy Clin. Immunol. 121:1108.
  2. Pestka, S. et al. (2004) Annu. Rev. Immunol. 22:929.
  3. Kotenko, S.V. et al. (1997) EMBO J. 16:5894.
  4. Spencer, S.D. et al. (1998) J. Exp. Med. 187:571.
  5. Sheikh, F. et al. (2004) J. Immunol. 172:2006.
  6. Hor, S. et al. (2004) J. Biol. Chem. 279:33343.
  7. Kotenko, S.V. et al. (2000) J. Biol. Chem. 276:2725.
  8. Xie, M.-H. et al. (2000) J. Biol. Chem. 275:31335.
  9. Kotenko, S.V. et al. (2003) Nat. Immunol. 4:69.
  10. Sheppard, P. et al. (2003) Nat. Immunol. 4:63.
  11. Yoon, S.I. et al. (2006) J. Biol. Chem. 281:35088.
  12. Pletnev, S. et al. (2005) BMC Struct. Biol. 5:10.
  13. Lutfalla, G. et al. (1993) Genomics 16:366.

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