
Interleukin-17A (IL-17A) belongs to the IL-17 family that contains IL-17A through IL-17F. They have a similar protein structure, with four highly conserved cysteine residues critical to their 3-dimensional shape, but no sequence similarity to any other known cytokines. Interleukin 17 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. Mature IL-17 containing one potential N-linked glycosylation site. Both recombinant and natural IL-17 have been shown to exist as disulfide linked homodimers. At the amino acid level, rat IL-17A exhibits 89 % amino acid identity with Mouse IL-17A. High levels of rat IL-17 were induced from primary peripheral blood CD4+ T cells upon stimulation and they can induce stromal cells to produce proinflammatory and hematopoietic cytokines.
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