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- W1997942721 abstract "Alzheimer’s disease (AD) is a neurodegenerative affliction associated with memory dysfunction. Senile plaques are a pathological hallmark of AD, and amyloid β (Aβ) peptides are a major component of these plaques. Aβ peptides are derived from proteolytic cleavage of the Aβ protein precursor (APP) by β- and γ-secretases to generate two principal species, Aβ1–40 and Aβ1–42. We have developed antibodies against the N- and C-termini of these peptides, and an ELISA for accurate and sensitive quantitative assessment. Sandwich ELISA composed of N-terminus (Aβ1) end-specific antibody, clone 82E1, and C-termini end-specific antibodies, and clones 1A10 and 1C3 for Aβ40 and Aβ42, respectively, detects full-length Aβ1–40 and 1–42 with a sensitivity in the sub single digit fmol/ml (equivalent to single digit pg/ml) range with no cross-reactivity to APP. A combination of C-termini antibodies and an antibody against the middle region of Aβ detects mouse Aβ in non-transgenic mouse brains." @default.
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- W1997942721 date "2004-07-01" @default.
- W1997942721 modified "2023-09-26" @default.
- W1997942721 title "P3-006 Endophenotypes in Alzheimer disease: nutritional, inflammatory and metal indices" @default.
- W1997942721 doi "https://doi.org/10.1016/s0197-4580(04)81161-8" @default.
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