Recombinant human Interleukin-17A (IL-17A) is produced in CHO cells in a tag-free format, ensuring native protein folding and human-like post-translational modifications, including critical glycosylation patterns. IL-17A is a disulfide-linked homodimeric cytokine and the prototypical member of the IL-17 family, primarily secreted by activated Th17 cells to coordinate local tissue inflammation and mucosal immunity.

In humans, IL-17A signals through a heteromeric receptor complex composed of IL-17RA and IL-17RC. This binding triggers the robust induction of pro-inflammatory cytokines, chemokines, and antimicrobial peptides—such as IL-6, TNF-α, and G-CSF—from various cell types, including epithelial cells, endothelial cells, and fibroblasts. The CHO-derived, tag-free expression system ensures that the protein maintains high specific bioactivity and batch-to-batch consistency, eliminating the risk of interference from affinity tags or improper folding.