Description: The monoclonal antibody H17F10A7 reacts with human IL-17F, a member of the IL-17 family of pro-inflammatory cytokines. Like IL-17A, IL-17F is a disulfide-linked, homodimeric glycoprotein. The IL-17F homodimer includes a classical cysteine knot motif, which is found also in the TGF-ß, BMP, and NGF superfamilies. The presence of the cysteine knot motif suggested the possibility of a heterodimeric structure, as was reported for TGF-ß and inhibin/activin. Recent reports confirm that co-expression of IL-17F and IL-17A in HEK293 cells results in the formation of biologically active IL-17F/IL-17A heterodimers, in addition to the IL-17F homodimers and IL-17A homodimers. Moreover, activated human CD4+ T cells were found to produce the IL-17A/F heterodimer, along with the corresponding homodimers. In comparing the relative potency of IL-17A, IL-17F, and IL-17A/F, all three were found to induce GRO-a secretion; IL-17A was most potent, followed by IL-17A/F heterodimer, then IL-17F (100fold lower than IL-17A). These heterodimers can be detected by immunoprecipitation with eBio64CAP17 anti-IL-17A monoclonal antibody followed by immunoblot with H17F10A7.