| Product Name | Beta-Amyloid (1-40) S26C |
| Catalog Number | LT9148 |
| Sequence | DAEFRHDSGYEVHHQKLVFFAEDVGCNKGAIIGLMVGGVV |
| Mutation | S26C |
| Molecular Weight | 4346.2 |
| Purity | ≥95% |
| Mechanism & Biological Significance | The S26C substitution introduces a cysteine within Aβ40 that can form a defined disulfide-linked dimer under oxidizing conditions, providing a controllable model for investigating the biological consequences of Aβ dimerization. |
| Published Research Context | Peer-reviewed studies directly synthesized and validated Aβ40 S26C by HPLC, mass spectrometry and amino-acid analysis, then oxidized the peptide to produce covalent dimers. S26C-derived dimers have been used in synaptic-plasticity, oligomer-standard and imaging studies. |
| Research Applications | - covalent Aβ dimer generation
- synaptic plasticity and toxicity studies
- Aβ oligomer assay standards
- thiol-selective labeling and conjugation research
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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 | - Amyloid β-protein dimers isolated directly from Alzheimer brains impair synaptic plasticity and memory
- Systematic analysis of time-dependent neural effects of soluble amyloid β oligomers
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