Interleukin-17A, (also known as CTLA-8) is a T cell-expressed pleiotropic cytokine that exhibits a high degree of homology to a protein encoded by the ORF13 gene of herpesvirus Saimiri. cDNA clones encoding IL-17 have been isolated from activated rat, mouse and human T cells. IL-17 represents a family of structurally-related cytokines that share a highly conserved C-terminal region but differ from one another in their N-terminal regions and in their distinct biological roles. The six known members of this family, IL-17A through IL-17F, are secreted as homodimers.
Recombinant murine IL-17A is a 15-20kDa glycosylated cytokine of 133 amino acid polypeptide chain that plays an important role in antimicrobial and chronic inflammation. IL-17 exhibits multiple biological activities on a variety of cells including the induction of IL-6 and IL-8 production in fibroblasts, the enhancement of surface expression of ICAM-1 in fibroblasts, activation of NF-?B and costimulation of T cell proliferation.