| Product Name | Beta-Amyloid (1-40), E22G Arctic Mutation |
| Catalog Number | LT9147 |
| Sequence | DAEFRHDSGYEVHHQKLVFFAGDVGSNKGAIIGLMVGGVV |
| Mutation | E22G |
| Molecular Weight | 4258.1 |
| Purity | ≥95% |
| Mechanism & Biological Significance | The Arctic E22G substitution removes the negatively charged Glu22 side chain and strongly promotes pathogenic Aβ assembly, protofibril formation and mutation-dependent misfolding. |
| Published Research Context | Exact E22G Aβ40 has been synthesized and analyzed in familial-mutation oligomerization studies and in cross-seeding experiments showing enhanced misfolding of E22G Aβ40 by wild-type Aβ42 fibril seeds. |
| Research Applications | - Arctic mutation research
- Aβ40 protofibril and fibril formation
- cross-seeding experiments
- solid-state NMR and amyloid structure studies
|
| 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
- E22G pathogenic mutation of β-amyloid enhances misfolding of Aβ40
|
