Mouse IL‑17/IL‑17A PerCP‑conjugated Antibody

Interleukin 17, also known as IL-17A and CTLA-8, was initially identified as a 17 kDa, secreted T cell-expressed pleiotropic cytokine that exhibits a high degree of homology to a protein encoded by the ORF13 gene of herpesvirus Saimiri. Mouse IL-17 cDNA encodes a 158 amino acid (aa) residue precursor protein with a 25 amino acid residue signal peptide that is cleaved to yield the 133 aa residue mature IL-17. Both recombinant and natural IL-17 have been shown to exist as disulfide linked homodimers. IL-17 is also known to form a heterodimer with IL-17F. At the amino acid level, mIL-17 shows 62% and 87% aa sequence identity with human and rat IL-17, respectively. The receptor for the IL-17A homodimer and IL-17A:F heterodimer is reported to be a combinationof IL-17 RA and IL-17 RC, with a possible contribution by IL-17 RD. The expression of IL-17 is widespread, and found associated with LTi cells, B cells, gamma delta T cells, CD4⁺ Th17 cells, iNKT cells, neutrophils, intestinal Paneth cells, Type I ILCs and CD8⁺ T_c17 cells. IL-17 exhibits multiple biological activities on a variety of cells including: the induction of IL-6 and IL-8 production in fibroblasts, the enhancement of surface expression of ICAM-1 in fibroblasts, activation of NF-kappa B and costimulation of T cell proliferation, the preservation of intestinal mucosal integrity, and the induction of antimicrobial peptides by epithelium.