Biological activity was measured by its ability to induce IL - 6 production by NIH 3T3 cells.
Properties
PURITY:
Greater than 98% by SDS-PAGE gel and HPLC analyses.
Endotoxin level is less than 0.1 ng per μg (1EU/μg).
PHYSICAL STATE:
Lyophilized
STORAGE CONDITIONS:
The lyophilized IL-17A recombinant protein is stable for at least 2 years from date of receipt at -20˚C. Reconstituted IL-17A is stable for at least 3 months when stored in working aliquots with a carrier protein at -20˚C. As with any protein, exposing IL-17A recombinant protein to repeated freeze / thaw cycles is not recommended. When working with proteins care should be taken to keep recombinant protein at a cool and stable temperature.
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.
Specifications
