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Originally identified as IL-17 and now referred to as IL-17A, this protein is a homodimer consisting of two 136 amino acid chains. It is released by activated T-cells and acts on stromal cells, triggering the production of proinflammatory and hematopoietic bioactive molecules. Today, IL-17 encompasses a family of structurally-related cytokines with a highly conserved C-terminal region. However, they vary in their N-terminal regions and exhibit distinct biological functions. The family includes six members known as IL-17A through IL-17F, all of which are secreted as homodimers.
Of note, IL-17A demonstrates bioactivity across species, showing effectiveness in both Human and murine cells. The recombinant Human IL-17A is a 31.3 kDa disulfide-linked homodimer composed of two 137 amino acid polypeptide chains.
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