The originally described IL-17 protein, now known as IL-17A, is a disulfide linked homodimer, 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. Recombinant murine IL-17A is a 30.0 kDa disulfide-linked homodimer of two 133 amino acid polypeptide chains.
Amino Acid Sequence
Measured by its ability to induce IL-6 production by NIH 3T3 cells.
Endotoxin level is <0.1 ng/μg of protein (<1EU/μg).
Centrifuge the vial prior to opening. Reconstitute in water to a concentration of 0.1–1.0 mg/ml. Do not vortex. This solution can be stored at 2–8°C for up to 1 week. For extended storage, it is recommended to further dilute in a buffer containing a carrier protein (example 0.1% BSA) and store in working aliquots at –20°C to –80°C.