IL-17D is a disulfide-linked homodimer of two 185 amino acid polypeptide chains. It belongs to the IL-17 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. 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 human IL-17D is a 40.5 kDa disulfide-linked homodimer of two 185 amino acid polypeptide chains.
IL-17D is a disulfide-linked homodimer of two 185 amino acid polypeptide chains. Recombinant human IL-17D is a 40.5 kDa disulfide-linked homodimer of two 185 amino acid polypeptide chains.
Interleukin-17D Human Recombinant (18-202) produced in E.Coli is a non-glycosylated disulfide-linked homodimer containing 2 polypeptide chains of 185 amino acids each and having a molecular mass of 40kDa.
The IL-17D is purified by proprietary chromatographic techniques.
IL17D modulates immune responses indirectly by stimulating the production of myeloid growth factors and chemokines, as well as suppressing the proliferation of myeloid progenitors. IL17D is expressed in the skeletal muscle, heart, adipose tissue, lung, pancreas, and nervous system. Among IL-17 family members, IL17D is most closely related to IL17B, sharing 27% aa sequence identity. The treatment of endothelial cells with IL17D cytokine stimulates the production of other cytokines including IL6, IL8 and CSF2/ GM-CSF. The increased expression of IL8 induced by IL17D cytokine is NF-kappa B-dependent.
