|Detection of Human IL‑10 R alpha by Western Blot. Western blot shows lysates of RPMI 8226 human multiple myeloma cell line. PVDF membrane was probed with 0.5 µg/mL of Mouse Anti-Human IL‑10 R alpha Monoclonal Antibody (Catalog # MAB2742) followed by HRP-conjugated Anti-Mouse IgG Secondary Antibody (Catalog # HAF007). A specific band was detected for IL‑10 R alpha at approximately 100 kDa (as indicated). This experiment was conducted under reducing conditions and using Immunoblot Buffer Group 1.|
|Detection of IL-10 R alpha in Human Blood Lymphocytes by Flow Cytometry. Human peripheral blood lymphocytes were stained with Mouse Anti-Human IL‑10 R alpha Monoclonal Antibody (Catalog # MAB2742) followed by Phycoerythrin-conjugated Anti-Mouse IgG Secondary Antibody (Catalog # F0102B) and Mouse Anti-Human CD19 APC-conjugated Monoclonal Antibody (Catalog # FAB4867A). Quadrant markers were set based on control antibody staining (Catalog # MAB0041).|
IL-10, initially designated cytokine synthesis inhibitory factor (CSIF), is a potent immunosuppressant of macrophage functions. IL-10 is also a pleiotropic cytokine with multiple immunostimulatory as well as immunosuppressive effects on a variety of other cell types. IL-10 binds specifically and with high affinity to cell-surface receptors. Mouse and human cDNA clones encoding the ligand-binding IL-10 receptor (IL-10 R) have been isolated. The IL-10 R mRNA has been detected in all cell types that are known to respond to IL-10. Human and mouse IL-10 receptors are structurally related to the IFN-gamma receptor. These receptors are members of the class II subgroup of the cytokine receptor superfamily. The deduced amino acid sequence of human IL-10 R is approximately 60% identical to mouse IL-10 R. Although human IL-10 has cross-species activities and is active on mouse cells, mouse IL-10 is species-specific in its actions and does not bind to the human IL-10 receptor. The human IL-10 R gene has been mapped to chromosome 11q23.3. Recombinant IL-10 soluble receptor, consisting of the extracellular domain of IL-10 R, binds IL-10 with high affinity in solution and is a potent IL-10 antagonist.
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