Amyloid β Peptides

Supporting information

Amyloid β (Aβ) peptides are the major component of amyloid plaques found in the brains of Alzheimer's patients. Aβ is formed from the progressive cleavage of amyloid precursor protein (APP) by β- and γ-secretase. Two Aβ peptides are formed from APP degradation; Aβ40 and Aβ42. Aβ40 is the most abundant form, but Aβ42 is more fibrillogenic, thus is associated with disease states.

Mutations in APP have been linked to early onset Alzheimer's disease, as proteolytic cleavage of the altered protein increases the levels of Aβ42 relative to Aβ40. Furthermore, Aβ proteins have been associated with other diseases including Lewy body dementia, inclusion body myositis and cerebral amyloid angiopathy.

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Gene Species Gene Symbol Gene Accession No. Protein Accession No.
APP1 Human APLP1 NM_001024807 P51693
Mouse Aplp1 NM_007467 Q03157
Rat Aplp1 H34623 -
APP2 Human APLP2 NM_001642 Q06481
Mouse Aplp2 NM_001102455 Q06335
Rat Aplp2 XM_343513 P15943

Literature for Amyloid β Peptides

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A collection of over 275 products for neurodegeneration research, the guide includes research tools for the study of:

  • Alzheimer's disease
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Neurodegeneration Product Guide
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Written by Alan Palmer and updated in 2015, this poster summarizes structural and functional changes observed in the progression of Alzheimer's disease (AD), as well as classic AD drug targets. The hypotheses behind the neurobiology of AD are discussed alongside the different stages in disease progression. Compounds available from Tocris are listed.

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Alzheimer's Life Science Poster

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Neurodegeneration Research Product Guide

Neurodegeneration Product Guide

Our Neurodegeneration guide highlights over 275 products for neurodegeneration research. Request copy or view PDF today.

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Alzheimer's Disease: Neurobiology and Drug Targets

Written by Alan Palmer

Alzheimer's Life Science Poster

Our Alzheimer's disease poster summarizes the structural and functional changes observed in the progression of this neurodegenerative disease. Request copy or view PDF today.

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