Recombinant Macaca fascicularis IL23A&IL12B Heterodimer Protein (Active)

IL-23 drives Th17 differentiation and sustains inflammatory responses in autoimmune and infectious disease models, making the cynomolgus macaque ortholog essential for translational immunology studies that bridge rodent findings to primate physiology. This heterodimeric cytokine, spanning residues 22–189 of IL-23A and 23–328 of IL-12B, demonstrates robust antibody binding with an EC50 of 0.77–0.93 ng/mL in functional ELISA and a KD of 0.27 nM by surface plasmon resonance, confirming native epitope presentation suitable for antibody development, validation panels, and as a coating antigen in cytokine detection assays. The dual-tag architecture (N-terminal 10×His, C-terminal Twin-Strep) facilitates oriented immobilization in receptor-binding studies and JAK/STAT signaling pathway experiments using primary cynomolgus PBMCs or engineered cell lines. Endotoxin levels below 1.0 EU/μg and >95% purity meet the stringent criteria required for cell-based functional assays—including Th17 polarization, T-cell activation, and cytokine secretion profiling—where LPS contamination would confound IL-23-specific immune responses.