TNFRSF10C functions as a decoy receptor that competitively sequesters TRAIL without transducing apoptotic signals, making it a critical tool for dissecting TRAIL pathway regulation in cancer biology. This recombinant construct spans the extracellular ligand-binding domain (aa 26–221), expressed in mammalian cells to preserve native disulfide bonding and glycosylation essential for proper TRAIL engagement. Functional validation demonstrates an ED50 of 0.56 ng/mL in inhibiting TRAIL-mediated cytotoxicity in L-929 fibroblasts, confirming robust competitive inhibition activity that supports use in ligand-binding interaction assays (SPR, BLI, ELISA), TRAIL-blocking antibody screening, and therapeutic antibody epitope mapping. The preparation satisfies purity and endotoxin criteria typical for cell-based assays, with greater than 95% purity by SDS-PAGE and endotoxin levels below 1.0 EU/μg, providing a suitable basis for drug discovery screens targeting TRAIL-decoy receptor interactions.
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