Description
Interleukin-19 (IL-19) is a novel cytokine that was initially identified during a sequence data base search aimed at finding potential Interleukin-10 homologs. Interleukin-19 shares 21% amino acid identity with IL-10. The exon/intron structure of IL-19 is similar to that of the human IL-10 gene, comprising five exons and four introns within the coding region of the IL-19 cDNA. IL-19 shares a receptor complex with IL-20, indicating that the biological activities of these two cytokines overlap and that both may play an important role in regulating development and proper functioning of the skin. Unlike IL-10, which forms an intercalated dimer, the molecule of IL-19 is a monomer made of seven amphipathic helices, A-G, creating a unique helical bundle.
Recombinant Human IL-19 produced in E.Coli is a single, non-glycosylated polypeptide chain containing 155 amino acids and having a molecular mass of 17913 Dalton. Recombinant Human Interleukin-19 is purified by proprietary chromatographic techniques