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 disulfide-linked homodimer with a total weight of 40.5 kDa, consisting of 370 amino acid residues.
Human IL17D expressed in E.coli
CAT# CSC-CTK0261-10 (10 μg); CAT# CSC-CTK0261-50 (50 μg)
Greater than 98% as determined by SDS-PAGE and HPLC analysis.
Less than 1 EU/μg.
Lyophilized (freeze-dried), sterile powder. Lyophilized with no additives.
Please centrifuge product briefly before opening vial. The lyophilized protein should be reconstituted in sterile, ultra-pure water to a concentration of 0,1 - 1,0 mg/ml. This solution can then be diluted into other aqueous buffers and stored at -20°C for future use.
Storage & Stability
The lyophilized protein, though stable at room temperature for up to 3 weeks, is best stored desiccated at -20°C. Reconstituted rHu IL-17D should be used immediately or stored long-term in undiluted working aliquots at -20°C. Avoid repeated freeze-thaw cycles.
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