| Product Name | Beta-Amyloid (1-40)-Lys(LC-biotin)-NH2, FAM-Labeled |
| Catalog Number | LT9143 |
| Product Quantity | 0.1 mg |
| Sequence | 5-FAM-DAEFRHDSGYEVHHQKLVFFAEDVGSNKGAIIGLMVGGVV-K(LC-BIOTIN)-NH2 |
| Molecular Weight | 5155.1 |
| Purity | ≥95% |
| Mechanism & Biological Significance | This dual-labeled amyloid-beta 40 reagent combines an N-terminal 5-FAM fluorophore with a C-terminal Lys(LC-biotin)-NH2 affinity handle. The Aβ40 sequence preserves the aggregation-prone amyloid core, while FAM permits fluorescence detection and the long-chain biotin handle permits streptavidin-based immobilization or capture. |
| Published Research Context | Published single-molecule studies used FAM-Aβ40-Lys-Biotin as a fluorescent, surface-tetherable Aβ40 probe. The peptide was immobilized through biotin-streptavidin chemistry and individual fluorescent species were analyzed by quantized photobleaching to resolve early Aβ oligomers. Follow-up work used the same probe architecture to study acid- and zinc-promoted oligomerization and to evaluate peptide-based inhibitors of Aβ assembly. |
| Research Applications | - single-molecule Aβ oligomer analysis
- amyloid aggregation and oligomerization studies
- streptavidin-based surface immobilization and capture
- fluorescence imaging and quantized photobleaching
- screening inhibitors of acid- or zinc-promoted Aβ assembly
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| Experimental Considerations | The N-terminal FAM label, LC-biotin handle, added lysine and C-terminal amide are integral to this construct and can alter aggregation or surface behavior relative to unlabeled Aβ40. Quantitative comparisons should therefore use preparation-matched controls and preserve the exact labeling and terminal chemistry. |
| Selected Scientific References | - Probing the efficacy of peptide-based inhibitors against acid- and zinc-promoted oligomerization of amyloid-β peptide via single-oligomer spectroscopy
- Monitoring the earliest amyloid-β oligomers via quantized photobleaching of dye-labeled peptides
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