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Fig. 1 | Molecular Neurodegeneration

Fig. 1

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

Fig. 1

Characterization of mouse 1C9 anti-tau2–18 monoclonal antibody. a Competition ELISA using peptides with Alanine substitution showed that 1C9 recognized epitope PRQEF comprising 4–8 amino acids of tau2–18 peptide. The half maximal inhibitory concentration (IC50) for each peptide is shown in Table. b 1C9 recognized full-length tau but not tau that lacks 2–18 domain in Western Blot. Lane 1- tauΔ2-18, lane 2-full-length tau. c 1C9 bound monomeric (spot 1), oligomeric (spot 2: cross-linked; spot 3: non-cross-linked) and fibrillar (spot 4) forms of recombinant tau protein in dot blot. d Anti-tau2–18 mAb 1C9 bound to neuropil threads and neurofibrillary tangles in AD brains (Braak stage VI-C). No binding was observed with non-AD brain (Braak stage 0). Original magnification 40X, scale bar = 20 μm. e 1C9 bound different species of tau protein in brain homogenates from both AD cases and control subjects in denaturing conditions (lane 1: control 1; lane 2-control 2; lane 3-AD1; lane 4-AD2; lane 5-AD3) in Western Blot. f In non-denaturing conditions in Dot Blots 1C9 as well as commercial TNT-1 Ab specific to N-terminus of Tau selectively bound to soluble tau in AD brains but not in controls. Of note, HT7 and rabbit anti-tau-polyclonal Ab recognizing total tau, had bound tau in both control and AD brains

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