Interleukin-17 (IL-17) is a family of pro-inflammatory cytokines that play a crucial role in the immune response. Among the IL-17 family, IL-17A and IL-17F are particularly significant due to their involvement in various inflammatory and autoimmune diseases. The IL-17A/F heterodimer is a unique combination of these two cytokines, exhibiting distinct biological activities compared to their homodimeric forms.
The IL-17A/F heterodimer is a disulfide-linked glycosylated protein composed of IL-17A and IL-17F subunits. In the case of the recombinant rat IL-17A/F heterodimer, it is produced using Chinese Hamster Ovary (CHO) cells. The recombinant protein is typically purified to a high degree of purity (>95%) and is free from endotoxins (<0.10 EU per 1 μg of the protein) .
The IL-17A/F heterodimer is biologically active and has been shown to induce the secretion of IL-6, a pro-inflammatory cytokine, in NIH-3T3 mouse embryonic fibroblast cells. The effective dose (ED50) for this activity ranges from 3 to 18 ng/mL . This activity is intermediate between the more potent IL-17A and the less potent IL-17F, highlighting the unique functional properties of the heterodimer.
IL-17A and IL-17F are known to be upregulated in various inflammatory conditions, including autoimmune diseases such as rheumatoid arthritis and psoriasis. The IL-17A/F heterodimer contributes to the pathogenesis of these diseases by promoting the recruitment and activation of neutrophils and other immune cells, leading to tissue inflammation and damage .
The recombinant rat IL-17A/F heterodimer is widely used in research to study its role in inflammation and immune responses. It serves as a valuable tool for investigating the signaling pathways and cellular mechanisms mediated by IL-17A and IL-17F. Additionally, it is used in the development of therapeutic strategies targeting IL-17-mediated diseases.