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Uncover the intricate dynamics of rIL17 A/F, a glycoprotein powerhouse secreted as a disulfide-linked heterodimer, merging the formidable forces of IL-17A and IL-17F within the IL-17 family. Characterized by a cysteine knot motif adorned with two disulfide bonds, proteins within the IL17 family exhibit remarkable structural complexity. Rat IL17A and IL17F, each originating as precursors, share significant sequence identity and N-linked glycosylation sites, underscoring their functional similarities. This dynamic duo, synthesized by activated CD4+ T cells, known as Th17, plays a pivotal role in immune regulation under the directive influence of IL-23. By forming heterodimers with IL17RA and IL17RC, rIL17 A/F facilitates binding interactions critical for immune modulation. Its potency, positioned between IL17A and IL17F, elicits chemokine production and airway neutrophilia, offering valuable insights into inflammatory processes. Delve into the versatile world of rIL17 A/F to advance your understanding of immune function and therapeutic strategies.