The cytokine Interleukin 27 (IL-27) is produced in response to inflammation. It is made by activated antigen presenting cells including monocytes, endothelial cells, and dendritic cells. IL-27 consists of a heterodimeric combination of Epstein-Barr virus-induced molecule 3 (EBI3, or IL-27B) non-covalently linked with IL-27 p28 (or IL-27A). It is a regulator of T helper cell development and suppressor of T-cell proliferation. IL-27 has both pro- and anti-inflammatory properties. It can stimulate cytotoxic T cell activity and induce isotype switching in B-cells. It has diverse effects on innate immune cells. It induces monocytes and mast cells to secrete pro-inflammatory cytokines. When infection is present, IL-27 induces naive CD4+ T cells to proliferate and develop Th1 cell responses. As an anti-inflammatory regulator, IL-27 can inhibit Th1 or Th2 responses and restrict the strength and duration of adaptive immune responses.
The IL-27 p28 subunit, a 28 kDa glycoprotein belonging to the type I cytokine family, is homologous to IL-12 p35, IL-23 p19, and IL-6. The EBI3 (Epstein-Barr virus-induced molecule 3, or IL-27B) subunit is a 34 kDa glycoprotein containing two fibronectin type III domains, and belongs to the type I cytokine receptor family. It can exist as a homodimer and can also heterodimerize with IL-12 p35. It is homologous to the p40 subunit of IL-12 and IL-23 and to the extracellular domain of IL-6 R. EBI3 can heterodimerize also with IL-12 p35, or can exist as a homodimer.
This antibody was prepared by repeated immunizations with recombinant mouse EBI3.