|Detection of IL‑10 by Western Blot. Western blot shows conditioned media from HEK293 human embryonic kidney cell line either mock transfected or transfected human IL-10. PVDF membrane was probed with 2 µg/mL of Mouse Anti-Human IL‑10 Monoclonal Antibody (Catalog # MAB9184) followed by HRP-conjugated Anti-Mouse IgG Secondary Antibody (Catalog # HAF018). A specific band was detected for IL‑10 at approximately 17 kDa (as indicated). This experiment was conducted under reducing conditions and using Immunoblot Buffer Group 1.|
|IL‑10 in Human PBMCs. IL‑10 was detected in immersion fixed human peripheral blood mononuclear cells (PBMCs) using Mouse Anti-Human IL‑10 Monoclonal Antibody (Catalog # MAB9184) at 25 µg/mL for 3 hours at room temperature. Cells were stained using the NorthernLights™ 557-conjugated Anti-Mouse IgG Secondary Antibody (red; Catalog # NL007) and counterstained with DAPI (blue). Specific staining was localized to cytoplasm. View our protocol for Fluorescent ICC Staining of Non-adherent Cells.|
Cell Proliferation Induced by IL‑10 and Neutralization by Human IL‑10 Antibody.
Recombinant Human IL‑10 (Catalog # 217-IL) stimulates proliferation in the MC/9‑2 mouse mast cell line in a dose-dependent manner (orange line) as measured by Resazurin (Catalog # AR002). Proliferation elicited by Recombinant Human IL‑10 (5 ng/mL) is neutralized (green line) by increasing concentrations of Mouse Anti-Human IL‑10 Monoclonal Antibody (Catalog # MAB9184). The ND50 is typically
Interleukin 10, also known as cytokine synthesis inhibitory factor (CSIF), is the charter member of the IL-10 family of alpha -helical cytokines that also includes IL-19,
IL‑20, IL-22, IL-24, and IL-26/AK155 (1, 2). IL-10 is secreted by many activated hematopoietic cell types as well as hepatic stellate cells, keratinocytes, and placental cytotrophoblasts (2‑5). Mature human IL-10 shares 72%‑86% amino acid sequence identity with bovine, canine, equine, feline, mouse, ovine, porcine, and rat IL-10. Whereas human IL-10 is active on mouse cells, mouse IL-10 does not act on human cells (6, 7). IL-10 is a 178 amino acid molecule that contains two intrachain disulfide bridges and is expressed as a 36 kDa noncovalently associated homodimer (6, 8, 9). The IL-10 dimer binds to two IL-10 R alpha /IL-10 R1 chains, resulting in recruitment of two IL-10 R beta /IL-10 R2 chains and activation of a signaling cascade involving JAK1, TYK2, and STAT3 (10). IL-10 R beta does not bind IL-10 by itself but is required for signal transduction (1). IL-10 R beta also associates with IL‑20 R alpha, IL-22 R alpha, or IL-28 R alpha to form the receptor complexes for IL-22, IL-26, IL-28, and IL‑29
(11‑13). IL-10 is a critical molecule in the control of viral infections and allergic and autoimmune inflammation (14‑16). It promotes phagocytic uptake and Th2 responses but suppresses antigen presentation and Th1 proinflammatory responses (2).
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