Recombinant Human IL-10 R beta Fc Chimera Protein, CF Summary
Details of Functionality
Measured by its binding ability in a functional ELISA. When Recombinant Human IL‑28 R alpha /IFN‑ lambda R1 Fc Chimera (Catalog # 5260-MR) is immobilized at 0.5 μg/well, the concentration of Recombinant Human IL-10 R beta Fc Chimera that produces 50% of the optimal binding response is found to be approximately 4-16 μg/mL.
Mouse myeloma cell line, NS0-derived human IL-10 R beta protein
Human IL-10 R beta (Met20-Ser220) Accession # Q08334
>95%, by SDS-PAGE under reducing conditions and visualized by silver stain
<0.01 EU per 1 μg of the protein by the LAL method.
51 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.
75-85 kDa, reducing conditions
Read Publication using 874-RB in the following applications:
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.
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