This product is an unconjugated, non-therapeutic recombinant analog of drozitumab, a fully human IgG1 monoclonal antibody directed against the death receptor DR5 (TNFRSF10B / TRAIL-R2). It is built around the drozitumab binding specificity and supplied for research use only; it is not the clinical drug and is not intended for human or veterinary use. Unlike neutralizing antibodies, drozitumab is an agonistic antibody that clusters DR5 to mimic TRAIL-driven death-receptor signaling, making this analog a useful tool for probing extrinsic apoptosis in tumor and other cell models. Researchers use it as a defined, reproducible reagent for target-engagement and binding assays, apoptosis-induction studies, receptor-clustering and crosslinking experiments, comparator or benchmark controls against other DR5 agonists, and as a building block for ADC or bispecific-format development. It is available at low-endotoxin research grade and ultra-low-endotoxin grades, and in bulk milligram-to-gram quantities to support assay scale-up, screening campaigns, and preclinical model work requiring consistent lot-to-lot material.
TNFRSF10B, better known as DR5 (also TRAIL-R2, KILLER, TRICK2), is a type I transmembrane death receptor of the TNF receptor superfamily and one of two signaling receptors for the cytotoxic ligand TRAIL (TNFSF10). Its extracellular region contains cysteine-rich domains that engage TRAIL, while its cytoplasmic death domain nucleates the extrinsic apoptotic pathway. Upon ligand binding or antibody-induced clustering, DR5 recruits the adaptor FADD and pro-caspase-8 to assemble the death-inducing signaling complex (DISC), activating caspase-8 and the downstream executioner caspase cascade. DR5 also contributes to NF-kappa-B activation and participates in endoplasmic-reticulum-stress-induced cell death. Because many tumor cells are sensitive to DR5-triggered apoptosis, DR5 has been a longstanding target for pro-apoptotic cancer therapeutics, and agonistic antibodies against it are widely studied research tools.