Recombinant Human IL-17F

The originally described IL-17 protein, now known as IL-17A, is a homodimer of two 155 amino acid chains, secreted by activated T-cells and acts on stromal cells to induce production of proinflammatory and hematopoietic bioactive molecules. Today, IL-17 represents a family of structurally-related cytokines that share a highly conserved C-terminal region and differ from one another in their Nterminal segments and in their distinct biological roles. The six known members of this family, IL-17A through IL-17F, are secreted as disulfide-linked homodimers. IL-17E has been shown to stimulate secretion of IL-8 and to induce activation of the transcription factor, NF-kB. Recombinant IL-17E is a disulfidelinked homodimer with a total weight of 33.8 kDa, consisting of 292 amino acid residues.