Recombinant Mouse IL-10 R beta Fc Chimera Protein, CF Summary
Details of Functionality |
Measured by its binding ability in a functional ELISA. When recombinant mouse (rm) IL-10 R alpha is present at 1 µg/mL, it binds rmIL-10 R beta Fc Chimera in the presence of rmIL-10. The concentration of rmIL-10 R beta Fc Chimera that produces 50% of the optimal binding response is approximately 0.25-1.25 μg/mL. |
Source |
Mouse myeloma cell line, NS0-derived mouse IL-10 R beta protein
Mouse IL-10 R beta (Ile21-Ser220) Accession # Q61190 |
IEGRMDP |
Mouse IgG2A (Glu98-Lys330) |
N-terminus |
|
C-terminus |
|
|
Accession # |
|
N-terminal Sequence |
Ile21 |
Structure / Form |
Disulfide-linked homodimer |
Protein/Peptide Type |
Recombinant Proteins |
Gene |
Il10rb |
Purity |
>95%, by SDS-PAGE under reducing conditions and visualized by silver stain |
Endotoxin Note |
<0.10 EU per 1 μg of the protein by the LAL method. |
Applications/Dilutions
Dilutions |
|
Theoretical MW |
50.5 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 |
70-80 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 and Trehalose. |
Purity |
>95%, by SDS-PAGE under reducing conditions and visualized by silver stain |
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 Mouse IL-10 R beta Fc Chimera Protein, CF
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 mouse IL-10 R beta consists of a 201 amino acid (aa) extracellular region with two fibronectin type-III domains, a 21 aa transmembrane segment and a 108 aa cytoplasmic domain (13). Within the ECD, mouse IL-10 R beta shares 75% and 87% aa sequence identity with human and rat IL-10 R beta , respectively.
- Commins, S. et al. (2008) J. Allergy Clin. Immunol. 121:1108.
- Pestka, S. et al. (2004) Annu. Rev. Immunol. 22:929.
- Kotenko, S.V. et al. (1997) EMBO J. 16:5894.
- Spencer, S.D. et al. (1998) J. Exp. Med. 187:571.
- Sheikh, F. et al. (2004) J. Immunol. 172:2006.
- Hor, S. et al. (2004) J. Biol. Chem. 279:33343.
- Kotenko, S.V. et al. (2000) J. Biol. Chem. 276:2725.
- Xie, M.-H. et al. (2000) J. Biol. Chem. 275:31335.
- Kotenko, S.V. et al. (2003) Nat. Immunol. 4:69.
- Sheppard, P. et al. (2003) Nat. Immunol. 4:63.
- Yoon, S.I. et al. (2006) J. Biol. Chem. 281:35088.
- Pletnev, S. et al. (2005) BMC Struct. Biol. 5:10.
- Gibbs, V.C. and D. Pennica (1997) Gene 183:97.
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