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• W2507267710 abstract "Amyloid-β42 (Aβ42) accumulates within senileplaque, a pathological hall mark ofAlzheimer’s disease (AD). Our previous reports showed that the monoclonal antibodies37-11 and 77-3 react with conformational epitopes on the surface of the solubleaggregates of Aβ42 and that sandwich ELISA using these two monoclonal antibodiesyields high reactivity to detect soluble aggregates of Aβ42. Here, the reactivity of thesandwich ELISA was shown to increase in the presence of 50 μM Cu2+. However, theaddition of Cu2+ had only a small effect on the reactivity of a direct ELISA using antibody37-11 or 77-3, suggesting that Cu2+ has a small effect on the number of epitopeson the surface of the aggregates. Atomic force microscopy images showed thatlarger aggregates were formed in the presence of Cu2+, as shown in the other reports.Cu2+ may gather the aggregates with distinct epitopes recognized by antibodies 37-11and 77-3, leading to increased signal intensity of the sandwich ELISA." @default.
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• W2507267710 date "2016-01-01" @default.
• W2507267710 modified "2023-09-26" @default.
• W2507267710 title "Copper Ions Enhance Signal Intensity of Sandwich ELISA for Amorphous Aggregates of Amyloid-β₄₂" @default.
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• W2507267710 doi "https://doi.org/10.4236/abb.2016.79033" @default.
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