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BN13 is a recombinant quadruple mutant of interleukin-13 (IL-13) featuring the specific amino acid substitutions E13K, R66D, S69D, and K105A. It was engineered to serve as a binding-null negative control in research targeting the interleukin-13 receptor subunit alpha-2 (IL13Rα2), a biomarker overexpressed in glioblastoma multiforme (GBM) and other malignancies. By disrupting the binding sites for both the physiological IL13Rα1/IL4Rα complex and the tumor-associated IL13Rα2, BN13 allows researchers to differentiate between specific receptor-mediated uptake and non-specific background accumulation in in vitro and in vivo studies. It was developed by researchers at the Wake Forest University School of Medicine to validate the specificity of high-affinity IL13Rα2 ligands like TQM13.
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