| Product Name | Beta-Amyloid (1-40), D7N Tottori Mutation |
| Catalog Number | LT9145 |
| Sequence | DAEFRHNSGYEVHHQKLVFFAEDVGSNKGAIIGLMVGGVV |
| Mutation | D7N |
| Molecular Weight | 4329.2 |
| Purity | ≥95% |
| Mechanism & Biological Significance | The Tottori D7N familial Alzheimer disease mutation replaces Asp7 with Asn in Aβ40, altering the N-terminal electrostatic environment and promoting faster conformational conversion and higher-order oligomer formation. |
| Published Research Context | Peer-reviewed work directly synthesized and characterized D7N Aβ40. D7N Aβ40 was evaluated by oligomerization, conformational, fibril and ion-mobility methods, providing exact-construct evidence for this 40-residue mutant. |
| Research Applications | - Tottori mutation research
- Aβ40 oligomer and fibril formation
- ion-mobility mass spectrometry
- familial Alzheimer disease structure-function studies
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| Experimental Considerations | Mutation identity and the Aβ C-terminal boundary are integral to this reagent. Compare with sequence-matched wild-type peptide using the same pretreatment, buffer, concentration, incubation time, and aggregation protocol. |
| Selected Scientific References | - Familial Alzheimer’s disease mutations differentially alter amyloid β-protein oligomerization
- Effects of the English (H6R) and Tottori (D7N) familial Alzheimer disease mutations on Aβ-protein assembly and toxicity
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