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Fig. 2 | Alzheimer's Research & Therapy

Fig. 2

From: Anti-β-sheet conformation monoclonal antibody reduces tau and Aβ oligomer pathology in an Alzheimer’s disease model

Fig. 2

Subcloned and purified anti-β-sheet conformational monoclonal antibody (aβComAb) GW-23B7-specific reactivity to human paired helical filaments (PHFs) and oligomeric Aβ peptides. a Enzyme-linked immunosorbent assay (ELISA) data showing the reactivity from cell supernatant of subcloned GW-23B7 immunoglobulin M (IgM) and an irrelevant clone from the same fusion to PHFs and oligomers differential on Aβ1–40 and Aβ1–42. The right panel shows the even coating of the selected peptides on the plate and the lack of unspecific reactivity to secondary antimouse IgM. b Western blots showing the pentameric integrity of the purified aβComAb GW-23B7. Lane 1 = unreduced sample, lane 2 = reduced with 0.1 M dithiothreitol (DTT). Left panel: Fast Green reversible protein stain. Middle panel: Antimouse IgM (μ-specific) light chain. Right panel: Antimouse kappa light chain. IgMp Pentameric immunoglobulin M, Hμr μ heavy chain reduced, Kr Kappa light chain reduced. c ELISA results showing the reactivity of purified aβComAb GW-23B7 diluted 1:1000 to Aβ1–40, Aβ1–42, and human PHFs. d Surface plasmon resonance showing the binding affinity of the purified aβComAb GW-23B7 to the oligomeric species of Aβ1–42 and the lack of binding affinity to the monomeric forms. The dissociation constant (KD) (14 nM) was determined from the raw data on the left

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