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- 2025年07月16日
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文献和实验Electrophoretic Separation and Immunoblotting of Aβ1–40and Aβ1–42
ending at amino acids 40 and 42, respectively (3 ). The longer form, Aβ42, aggregates more rapidly in vitro (4 ) and is preferentially deposited in vivo (3 ,5,6 ). Normally, Aβ is secreted as an apparently soluble molecule (7 -9 ). It is generated
Quantifying Aβ1–40 and Aβ1–42 Using Sandwich-ELISA
with autosomal penetrance (reviewed in ref . 1 ). Several of these FAD-associated APP mutations, as well as FAD-associated mutations in the presenilin 1 (PS1) and presenilin 2 (PS2) genes, lead to an increase in the production of Aβ1 –42 relative to Aβ1 _40
at amino acid Ala-42. Due to the tendency of the longer Aβ peptides to more readily form fibrils (7 ), these may accelerate Aβ deposition, which ultimately leads to more aggressive, early onset forms of Alzheimer’s disease (8 ). With the transgenic
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