Add 0.2 mL of distilled water, will yield a concentration of 500 µg/mL.
Interleukin-12 (IL-12) is a heterodimeric 70 kD (p70) cytokine composed of two covalently linked, glycosylated chains, 40kD (p40) and 35-kD (p35). IL-12 is mainly produced by monocytes, macrophages, and dendritic cells in response to bacterial products such as lipopolysaccharides (LPS), to intracellular pathogens or upon interaction with activated T cells. IL-12 was originally discovered because of its ability to induce interferon-gamma production, cell proliferation, and cytotoxicity mediated by natural killer cells and T cells. It is now established that IL-12 also plays a key role in the development of Th1 responses, leading to IFN-gamma and IL-2 production. These cytokines can in turn promote T-cell responses and macrophage activation. The p40 and p35 subunits by themselves have no IL-12 bioactivity, though the p40 homodimer has been shown to bind the IL-12 receptor and to be an antagonist of IL-12 p70. Free p40 is typically secreted in vast excess of IL-12 p70 by cells co-expressing both the p35 and p40 subunits. The p40 subunit of IL-12 has been shown to have extensive amino acid sequence homology to the extracellular domain of the IL-6 receptor, while the p35 subunit shows some homology to IL-6 and G-CSF.
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Protein Aliases: CLMF p40; Cytotoxic lymphocyte maturation factor 40 kDa subunit; IL-12 subunit p40; IL-12B; interleukin-12 p40; Interleukin-12 subunit beta
Gene Aliases: Il-12b; Il-12p40; Il12; Il12b; Il12p40; p40
UniProt ID: (Mouse) P43432