Recombinant Macaca fascicularis cytokine receptor-like factor 2 (CRLF2), partial (Active)

CRLF2 forms a heterodimeric receptor complex with interleukin-7 receptor alpha (IL-7Rα) to mediate thymic stromal lymphopoietin (TSLP) signaling, a pathway central to allergic inflammation and lymphocyte development. This cynomolgus macaque ortholog, spanning the extracellular ligand-binding domain (aa 23–231), demonstrates quantifiable binding to recombinant TSLP in functional ELISA with an EC50 of 2.698–3.710 ng/mL, providing a validated basis for ligand-receptor interaction studies, competitive inhibition assays, and therapeutic antibody epitope mapping in translational immunology research. Mammalian cell expression preserves the native glycosylation and disulfide architecture required for physiologically relevant TSLP recognition, supporting its use in surface plasmon resonance and biolayer interferometry experiments to characterize binding kinetics of anti-CRLF2 biologics or small-molecule modulators. The protein meets purity (>95% by SDS-PAGE) and endotoxin (<1.0 EU/μg) thresholds typical for quantitative binding assays and serves as a positive control in screening campaigns targeting the TSLP–CRLF2–IL-7Rα axis in allergic disease models.