|IL‑10 R alpha in Human PBMCs. IL‑10 R alpha was detected in immersion fixed human peripheral blood mononuclear cells (PBMCs) using 15 µg/mL Goat Anti-Human IL‑10 R alpha Antigen Affinity-purified Polyclonal Antibody (Catalog # AF‑274‑NA) for 3 hours at room temperature. Cells were stained (red) and counterstained (green). View our protocol for Fluorescent ICC Staining of Non-adherent Cells.|
IL‑10 Inhibition of IL‑1 beta secretion and Neutralization by Human|
IL‑10 R alpha Antibody. Recombinant Human IL‑10 (Catalog # 217-IL) inhibits IL‑1 beta secretion in LPS-activated human peripheral blood mononuclear cells (PBMC) in a dose-dependent manner (orange line), as measured by the Human
IL‑1 beta /IL‑1F2 Quantikine ELISA Kit (Catalog # DLB50). IL‑1 beta secretion inhibited by Recombinant Human
IL‑10 (0.25 ng/mL) is neutralized (green line) by increasing concentrations of Goat Anti-Human IL‑10 R alpha Antigen Affinity-purified Polyclonal Antibody (Catalog #
AF-274-NA). The ND50 is typically 20-40 µg/mL in the presence of LPS (0.25-3 ng/mL).
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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Immunoprecipitaiton with the Human IL-10 Rα antibody (Catalog # AF-274-NA) followed by western blotting for Human IL-10 Rα produces a 150 kDa band. What is the identity of this band?
Human IL-10 Rα antibody has not been validated for immunoprecipitaiton application. The MW of Human IL-10 Rα is about 90-110 kDa and the receptor binds with high affinity to the IL-10 homodimer, which has a MW of 40 kDa. Under non-denaturing conditions, the IL-10Rα may be complexed with IL-10 homodimer to give a 150 kDa band.