Human IL-17A protein is a homodimer consisting of two 134 amino acids peptides. IL-17A is secreted mainly by activated CD4+ and CD8+ T lymphocytes and acts through its receptor, IL-17R, to induce the expression of many mediators of inflammation, most strikingly, those that are involved in the proliferation, maturation and chemotaxis of neutrophils. Recombinant Human Interleukin-17-A (rHu IL-17-A) produced in E. coli is a homodimeric, non-glycosylated polypeptide chain that contains a total of 264 amino acids and has a molecular mass of 30.25 kDa. rHu IL-17-A consists of monomers and dimers at an approximate ratio of 50:50.