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Recombinant human IL-17 produced in E.coli is a 31.0kDa disulfide-linked homodimer of two 136 amino acid polypeptide chains.
The ED50 as determined by the dose-dependent induction of IL-6 in Hs68 cell line was found to be approximately 2ng/ml, corresponding to a specific activity of 5.0 x 105 IU/mg.
Less than 1 IEU/ug determined by LAL test.
>95% as determined by SDS-PAGE.
Lyophilized rHuIL-17 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution rHuIL-17 should be stored at 4°C between 2-7 days and for future use below -18°C. Aliquot to avoid repeated freeze-thaw cycles.
It is recommended to reconstitute the lyophilized rHuIL-17 in sterile 18MΩ-H2O containing at least 0.1% human serum albumin or bovine serum albumin to prepare a stock solution of no less than 100ug/ml of the cytokine.
The originally described IL-17 protein, now known as IL-17A, is a homodimer of two 132 amino acid chains, secreted by activated T-cells that act 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 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-17A exhibits cross-species bioactivity between human and murine cells.
Induces stromal cells to produce proinflammatory and hematopoietic cytokines. Enhances the surface expression of the intracellular adhesion molecule-1 (ICAM-1) in fibroblasts.