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Fig. 2 | Molecular Neurodegeneration

Fig. 2

From: Humanized monoclonal antibody armanezumab specific to N-terminus of pathological tau: characterization and therapeutic potency

Fig. 2

a SDS-PAGE analyses of purified antibody, Lane 1: Armanezumab, reducing conditions, 2.00 μg; Lane 2: Armanezumab, non-reducing conditions, 2.00 μg. b Armanezumab purified from CHO cells supernatant had a 99% purity measured by HPLC. c Characterization of Armanezumab and parental mouse 1C9 mAb by Surface Plasmon Resonance (SPR). SPR sensorgrams showing the binding of human tau (0 N/4R isoform) with each of immobilized antibody. Tau protein was run with various concentrations (3, 9, 27, 81, 243 nM), curves and fitted curve are shown in the corresponding color. Table shows the association rate constant (Ka), dissociation rate constant (Kd), and binding constant (KD) of antibodies with human tau. Biacore T200 evaluation software, version 1.0 was used to calculate Ka and Kd using 1:1 fitting model. Ms, millisecond; M, molar; s, second

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