IL-17F, a member of the IL-17 family of structurally related cytokines, has been shown to stimulate the proliferation and activation of T-cells and PBMCs. IL-17F also regulates cartilage matrix turnover and inhibits angiogenesis. The mature human IL-17F is a homodimeric protein with a total weight of 30.1 kDa, consisting of two 133 amino acid residue chains. E.coli-derived Recombinant Human IL-17F is a biologically active, non-glycosylated, disulfide-linked homodimeric protein containing 268 amino acids (30.1 kDa), including N-terminal methionine residues.
Amino Acid Sequence
Measured by its ability to induce IL-6 production by NHDF cells.
Endotoxin level is <0.1 ng/μg of protein (<1EU/μg).
Centrifuge the vial prior to opening. Reconstitute in water to a concentration of 0.1–1.0 mg/ml. Do not vortex. This solution can be stored at 2–8°C for up to 1 week. For extended storage, it is recommended to further dilute in a buffer containing a carrier protein (example 0.1% BSA) and store in working aliquots at –20°C to –80°C.
Cytokines and chemokines and related molecules
Interleukins 17F (IL-17F) and 17A (IL-17A) are closely related members of the IL-17 cytokine family, sharing about 50% amino acid identity. Studies in the mouse have identified Th17 cells as a distinct CD4+ T cell lineage that is defined by the production of IL-17F and IL-17A. IL-6 and transforming growth factor-β are required for the differentiation of naïve CD4+ T cells to Th17 cells, which are maintained in the presence of IL-23 and IL-1β. Conversely, IL-4 and interferon-γ can inhibit the development of Th17 cells. Th17 cells have been implicated in the pathology of mouse autoimmune disease models. Expression of IL-17F and IL-17A has been detected in activated Human peripheral blood lymphocytes. It has been shown that the cytokines are expressed in activated Human CD4+ T cells. Expression of IL-17F and IL-17A has also been observed in tissue samples from various autoimmune diseases such as rheumatoid arthritis, multiple sclerosis, psoriasis, inflammatory bowel disease, and asthma. The crystal structure of IL-17F has been solved and shows that the protein forms a disulfidelinked dimeric glycoprotein. IL-17A is also a disulfide-linked homodimeric glycoprotein. The IL- 17F homodimer includes a classical cysteine knot motif, which is found in the TGF-β, bone morphogenetic protein, and nerve growth factor superfamilies. One difference in the cysteine knot motif of IL-17F compared with the other known cysteine knot protein families is that it only utilizes four cysteines instead of the classical six cysteines to form the knot. IL-17F and IL-17A have been shown to form biologically active IL-17F/IL-17A heterodimers, in addition to the IL- 17F and IL-17A homodimers.