Recombinant Human IL12P40&IL12P35 Heterodimer Protein (Active)

IL-12 orchestrates Th1 polarization and NK cell activation through a tightly regulated heterodimeric architecture, making functional integrity essential for mechanistic studies of cell-mediated immunity. This tag-free heterodimer, spanning residues 23–328 of IL-12p40 and 23–219 of IL-12p35, demonstrates potent bioactivity with an ED50 below 0.5 ng/mL in NK-92 interferon-gamma secretion assays, directly validating its capacity to drive downstream JAK-STAT signaling and effector cytokine production. The endotoxin specification of ≤10 EU/mg meets the quality thresholds commonly required for primary immune cell activation studies, PBMC differentiation experiments, and in vivo inflammation models where LPS contamination would confound cytokine-specific responses. Purity exceeding 95% by SDS-PAGE, combined with the demonstrated NK cell activation profile, supports use as a positive control in cytokine detection platforms and as a functional reference in antibody validation workflows targeting the assembled p70 heterodimer.