Fig. S1. Monovalent binding affinity of mAR9.6 and huAR9.6 Fab fragments to recombinant MUC16 SEA domain fragments. (A) Representative SPR sensograms of the interaction of mAR9.6 and huAR9.6 Fab fragments with MUC16 fragments (Trx-1.2TR, SEA5, glycosylated 1.2TR) immobilized on a CM5 sensor chip; (B) Representative SPR sensograms of the interaction of huAR9.6 Fab with MUC16 fragments (glycosylated 1.7TR and glycosylated SEA10-15) immobilized on CAP S and CM5 sensor chips; (C) Representative SPR sensograms of the interaction of MUC16 captured from OVCAR-3 cell supernatant using anti-MUC16 IgG (B43.13/3A5 or huAR9.6) immobilized on a CM7 sensor chip. HuAR9.6 Fab or anti-EGFR VHH (control) were flowed over the surfaces. In all sensograms black lines represent raw data points; red lines are fits to a 1:1 binding model.
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Aguilar et al. (2024) studied this question.
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