Recombinant Human IL-10 R beta Fc Chimera Avi Protein, CF Summary
Additional Information |
Avi-tag |
Details of Functionality |
Measured by its binding ability in a functional ELISA. Biotinylated
Recombinant Human IL-10 R beta Fc Chimera Avi-tag (Catalog # AVI11460) 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) with an ED 50 of 50.0-750 ng/mL. |
Source |
Chinese Hamster Ovary cell line, CHO-derived human IL-10 R beta protein Human IL-10RB (Met20-Ser220) Accession # Q08334.2 | GGIEGRMD | Human IgG1 (Pro100-Lys330) | Avi-tag | N-terminus | | | C-terminus | |
|
N-terminal Sequence |
Met20 |
Structure / Form |
Disulfide-linked homodimer Biotinylated via Avi-tag |
Protein/Peptide Type |
Recombinant Proteins |
Endotoxin Note |
<0.10 EU per 1 μg of the protein by the LAL method. |
Applications/Dilutions
Dilutions |
|
Theoretical MW |
52 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 |
78-88 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. |
Reconstitution Instructions |
Reconstitute at 250 μg/mL in sterile water. |
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 Avi 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 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. Our Avi-tag Biotinylated human IL-10 R beta 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.
- 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.
- Lutfalla, G. et al. (1993) Genomics 16:366.
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