Interleukin-12 (IL-12) is, when biologically active, a heterodimer (p70) consisting of two covalently linked subunits, p35 and p40. IL-12 is produced by antigen-presenting cells, specifically dendritic cells and macrophages. IL-12 is a proinflammatory cytokine that promotes Th1-type responses by inducing IFN-γ production and enhancing proliferation and cytotoxicity of NK and T cells.
Interleukin-23 (IL-23) is a disulfide-linked heterodimer which consists of a unique p19 subunit and the p40 subunit of IL-12. IL-23 is a proinflammatory cytokine, which is produced by macrophages and dendritic cells upon infections with certain pathogens. The IL-23 receptor is expressed on Th17 cells and IL-23 is responsible for Th17 expansion and stabilization.
Since both IL-12 and IL-23 heterodimers comprise the p40 subunit, capture immunoassays based on antibodies to p40 will detect both cytokines. Such assays can also detect p40 monomers and dimers.
Rat monoclonal antibody specific for the p40 subunit of mouse Interleukin-12 and Interleukin-23, clone C15.6. Suitable as capture antibody in ELISA and ELISpot. When used in combination with biotinylated mAb clone C17.8 (code 3451-6), the antibody detects total IL-12 (i.e. monomer and homodimer of p40 and p70 heterodimer) and IL-23.