Recombinant Human IL-17D

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 N-terminal 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-17D has the ability to stimulate the production of IL-6, IL-8 and GM-CSF and inhibits hemopoiesis of myeloid progenitor cells in colony forming assays. Recombinant IL-17D is a disulfidelinked homodimer with a total weight of 40.5 kDa, consisting of 370 amino acid residues.