OX40 (TNFRSF4) is a costimulatory immune checkpoint receptor whose engagement with OX40L drives T cell survival and effector function, making it a high-priority target in immuno-oncology drug development. This recombinant human OX40 construct spans the extracellular ligand-binding domain (aa 29–216) with a C-terminal Fc tag, and its conformational integrity is confirmed by BLI-measured KD values of 70.3 nM against human OX40L and 165 nM against cynomolgus OX40L, supporting use in cross-species ligand-binding assays, therapeutic antibody epitope mapping, and competitive blocking antibody screening. Mammalian cell expression preserves native glycosylation and disulfide bonding critical for proper cysteine-rich domain folding, ensuring reliable performance as a positive control in BLI or SPR affinity characterization and in small-molecule or biologic inhibitor screening campaigns. Purity exceeding 95% by SDS-PAGE combined with endotoxin levels below 1.0 EU/μg satisfies the criteria typical for cell-based immune checkpoint functional assays.
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