Recombinant Macaca fascicularis Interleukin 1 receptor accessory protein(IL1RAP), partial (Active)

IL1RAP serves as an essential co-receptor in the IL-1 signaling complex, where it amplifies inflammatory responses by stabilizing the interaction between IL-1 and its primary receptor—a mechanism central to both innate immunity and chronic inflammatory disease models. This mammalian-expressed construct spanning residues 21–359 captures the complete extracellular ligand-binding domain, preserving the native glycosylation and disulfide architecture required for physiological receptor assembly. Functional ELISA validation demonstrates specific antibody binding with an EC50 of 0.91–1.18 ng/mL, confirming conformational integrity suitable for therapeutic antibody epitope mapping, competitive inhibition screening, and blocking antibody validation in drug discovery programs targeting IL-1 pathway dysregulation. The protein meets the purity and endotoxin criteria typical for quantitative binding assays including surface plasmon resonance, biolayer interferometry, and ELISA-based ligand-receptor interaction studies, with >95% purity by SDS-PAGE and <1.0 EU/μg endotoxin.