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Details
The Osaka mutation was the first deletion-type mutation to be identified in APP and Aβ.
The Aβ E22delta mutant is more resistant to degradation by two major Aβ-degrading enzymes, neprilysin and insulin-degrading enzyme. Synthetic mutant Aβ showed unusual aggregation properties with enhanced oligomerization but no fibrillization. It also inhibited hippocampal long-term potentiation more efficiently than wild-type Aβ. A transgenic mouse model containing APP with the E693delta mutation has been developed. APP(OSK)-Tg mice exhibit intraneuronal Aβ E22delta oligomers and memory impairment as early as eight months of age.
The Aβ E22delta mutant is more resistant to degradation by two major Aβ-degrading enzymes, neprilysin and insulin-degrading enzyme. Synthetic mutant Aβ showed unusual aggregation properties with enhanced oligomerization but no fibrillization. It also inhibited hippocampal long-term potentiation more efficiently than wild-type Aβ. A transgenic mouse model containing APP with the E693delta mutation has been developed. APP(OSK)-Tg mice exhibit intraneuronal Aβ E22delta oligomers and memory impairment as early as eight months of age.
Catalog Number
H-7474
One Letter Code
DAEFRHDSGYEVHHQKLVFFADVGSNKGAIIGLMVGGVV
Synonyms
Amyloid β-Protein (1-40) Osaka or Japanese Mutation, Amyloid β-Protein (1-40) E22Δ
Molecular Formula
C₁₈₉H₂₈₈N₅₂O₅₅S
Relative Molecular Mass
4200.75
CAS Registry Number
[1678416-36-8] net
Source
Synthetic
Storage Conditions
-20 ± 5 °C
Areas of Interest
Alzheimer's Disease
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