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

Interleukin 17 (IL-17), also known as IL-17A and CTLA-8, is a T cell-expressed pleiotropic cytokine that exhibits a high degree of homology to a protein encoded by the ORF13 gene of herpes virus Saimiri. cDNA clones encoding IL-17 have been isolated from activated rat, mouse and human T cells. Mouse IL-17 cDNA encodes a 158 amino acid (aa) residue precursor protein with a 26 amino acid residue signal peptide that is cleaved to yield the 132 aa residue mature  IL-17. Both recombinant and natural IL-17 have been shown to exist as disulfide linked homodimers and IL-17 is typically found as a heterodimer with IL-17F. At the amino acid level, mouse IL-17 shows 57%, 61%, and 87% sequence identity with herpes virus, human, and rat IL-17, respectively. An IL-17 specific mouse cell surface receptor (IL-17 R) has been cloned. While the expression of IL-17 mRNA is restricted to activated alpha beta TCR⁺CD4^-CD8^- T cells, the expression of mouse IL-17 R mRNA has been detected in virtually all cells and tissues tested. IL-17 has multiple biological effects on a variety of cells including the induction of IL-6 and IL-8 production by fibroblasts, the enhancement of surface expression of ICAM-1 on fibroblasts, and the activation of NF-kappa B and costimulation of proliferation by T cells.