Interleukin-17A/F Heterodimer, rat recombinant (rrIL-17A/F)

Rat recombinant IL-17A/F produced in E.coli is a heterodimeric, non-glycosylated polypeptide chain containing 1 monomeric subunit of each IL-17A and IL-17F. The dimer contains 271 amino acids. Rat IL-17A/F is a glycoprotein which is secreted as a disulfide-linked heterodimer. IL-17A/F consists of two proteins of the IL-17 family, IL-17A and IL17F. Proteins of the 6 homodimeric IL-17 family show a cysteine knot motif that contains two disulfide-bonds. Rat IL-17A is produced as a 155 amimo acid precursor that includes a 23 amino acids signal sequence and a 132 amino acid chain that includes an N-linked glycosylation site. Rat IL-17F is produced as a 153 amino acid precursor with a 20 amino acid signal sequence and a 133 amino acid region. Similar to IL-17A, IL-17F also has an N-linked glycosylation site. Both proteins (IL-17A and IL-17F) share 50% amino acid sequence identity. Human IL-17A and IL-17F show approximately 60% homology in their amino acid sequence to mouse IL-17A and IL-17F. Interleukin-17A/F and IL-17A, IL-17F homodimers are manufactured by activted CD4 T-cells, called Th17. IL-23 causes Th17 lymphocytes to manufacture IL-17A/F. IL17RA and IL17RC form a heterodimer for the binding of IL-17A and IL-17F. IL-17A/F binds IL-17RA. Interleukin-17A/F induces chemokine production and airway neutrophilia with intermediate potency between IL17A (most potent) and IL17F (least potent).