|IL‑17 Secretion Induced by IL‑23 and Neutralization by Human IL‑12/IL‑23 p40 Antibody. In the presence of Recombinant Mouse IL‑2 (10 ng/mL, Catalog # 402-ML), Recombinant Human IL‑23 (Catalog # 1290-IL) stimulates IL‑17 secretion in mouse splenocytes in a dose-dependent manner (orange line), as measured by the Mouse IL‑17 Quantikine ELISA Kit (Catalog # M1700). Under these conditions, IL‑17 secretion elicited by Recombinant Human IL‑23 (0.75 ng/mL) is neutralized (green line) by increasing concentrations of Human IL‑12/IL‑23 p40 Monoclonal Antibody (Catalog # MAB1510). The ND50 is typically 0.02-0.1 µg/mL. This antibody also neutralizes Human IL-12 induced activity in human PBLs. The ND50 is approximately 0.05-0.25 μg/mL in the presence of 1 ng/mL Recombinant Human IL-12.|
Interleukin 12, also known as natural killer cell stimulatory factor (NKSF) or cytotoxic lymphocyte maturation factor (CLMF), is a pleiotropic cytokine originally identified in the medium of activated human B lymphoblastoid cell lines. IL-12 is produced by macrophages and B lymphocytes and has multiple effects on T-cells and NK cells, including stimulation of cytotoxic activity, proliferation, and promotion of Th1 development as well as IFN-gamma and TNF production. IL-12 is a disulfide-linked, 70 kDa (p70) heterodimeric glycoprotein composed of a 40 kDA (p40) subunit and a 35 kDa (p35) subunit. The p40 and p35 subunits by themselves have no IL-12 activity, the p40 dimer has been shown to bind the IL-12 receptor and to be an IL-12 antagonist. Free p35 has not been detected in supernatant solutions of cultured cells expressing only p35 or both p35 and p40 mRNAs. In contrast, p40 is secreted in excess of IL-12 in cells expressing both p35 and p40 mRNAs. The p40 subunit of IL-12 has been shown to have extensive amino acid sequence homology to the extracellular domain of the human IL-6 receptor while the p35 subunit shows distant but significant sequence similarity to IL-6, G-CSF, and chicken MGF. These observations have led to the suggestion that IL-12 might have evolved from a cytokine/soluble receptor complex. Human and mouse IL-12 share 70% and 60% amino acid sequence homology in their p40 and p35 subunits, respectively. IL-12 apparently shows species specificity with human IL-12 reportedly showing minimal activity in the murine system.
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