TNFRSF10B (DR5/Killer) serves as a critical death receptor in TRAIL-mediated apoptosis, making it a key target in cancer biology and therapeutic antibody development. This recombinant mouse Fc-tagged construct covers the extracellular ligand-binding domain (aa 53–177) and demonstrates functional activity with an ED50 of 92.04 ng/mL in inhibiting TRAIL-mediated cytotoxicity in L-929 fibroblasts at 40 ng/mL TNFSF10, confirming its suitability for competitive inhibition assays, blocking antibody screening, and ligand-binding interaction studies via ELISA, SPR, or BLI. Mammalian cell expression preserves native glycosylation and proper disulfide-mediated folding of the cysteine-rich extracellular domain, supporting conformational integrity essential for epitope mapping and small-molecule or biologic inhibitor screening in drug discovery workflows. Purity exceeding 95% by SDS-PAGE combined with endotoxin levels below 1.0 EU/μg satisfies the quality criteria typical for cell-based functional assays and affinity characterization experiments.
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