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

CRLF2 forms a heterodimeric receptor complex with IL-7Rα and mediates TSLP signaling, a pathway implicated in allergic inflammation and certain B-cell acute lymphoblastic leukemias. This recombinant protein, spanning the extracellular domain (aa 23–231) and produced in mammalian cells to preserve native glycosylation and disulfide bonding, demonstrates quantifiable antibody-binding activity with an EC50 of 2.079–2.450 ng/mL in functional ELISA, confirming conformational integrity suitable for therapeutic antibody epitope mapping, competitive inhibition screening, and blocking antibody validation. The low endotoxin level (less than 1.0 EU/μg) and greater than 95% purity meet the quality thresholds commonly required for ligand-binding assays, surface plasmon resonance affinity characterization, and biolayer interferometry studies. Researchers investigating TSLP-driven immune responses or developing biologics targeting the CRLF2–IL-7Rα axis can use this protein as a positive control in binding assays or as an immobilized ligand for screening small-molecule or biologic inhibitors.