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Amyloid β-Protein (1–42), Human, commonly abbreviated Aβ42, is one of the principal amyloid-β species generated through APP processing and one of the most extensively investigated peptides in Alzheimer’s disease research.
Compared with Aβ40, Aβ42 contains the additional hydrophobic residues Ile41 and Ala42, which substantially influence its self-assembly behavior.
Product Information
| Property | Specification |
|---|---|
| Product Name | Amyloid β-Protein (1–42), Human |
| Sequence | DAEFRHDSGYEVHHQKLVFFAEDVGSNKGAIIGLMVGGVVIA |
| Length | 42 amino acids |
| Molecular Formula | C203H311N55O60S |
| Theoretical MW | ~4514.11 Da |
| Species | Human |
| Peptide Type | Amyloid-β peptide |
| Research Areas | Oligomers, fibrils, aggregation, membrane interactions, amyloid biology |
Research Applications
Human Aβ42 is widely used in studies of peptide self-assembly, oligomer formation, fibrillation, membrane interaction, antibody recognition, aggregation inhibitors and amyloid-associated cellular responses.
It also serves as the primary wild-type comparator for several important Aβ42 analogs and disease-associated sequence variants.
Purity Does Not Define Aggregation State
For Aβ42, analytical purity is only one part of experimental reproducibility.
Two samples with the same HPLC purity can behave differently if their reconstitution, monomerization, incubation or storage histories differ.
We therefore recommend documenting solvent history, concentration, pH, ionic strength, temperature and incubation time for experiments in which oligomeric or fibrillar state is important.
Additional analytical considerations are available through Peptide Quality Control and Recommended Peptide Purity.
Frequently Asked Questions
What is human Aβ42?
Human Amyloid β-Protein (1–42), or Aβ42, is a 42-residue APP-derived peptide widely used to study amyloid aggregation, oligomer formation, fibrils, membrane interactions, and Alzheimer-associated molecular mechanisms.
What is the difference between Aβ40 and Aβ42?
Aβ42 contains two additional C-terminal residues, Ile41 and Ala42. These residues increase hydrophobicity and strongly influence self-assembly, making Aβ42 generally more aggregation-prone than Aβ40 under comparable conditions.
Why can two Aβ42 experiments give different results even when the peptide purity is the same?
Aβ42 behavior is highly sensitive to its physical state. Solvent history, monomerization procedure, concentration, ionic strength, incubation time, temperature, and freeze–thaw history can change the relative amounts of monomeric, oligomeric, and fibrillar material.
What should be recorded when using Aβ42 in aggregation studies?
In addition to sequence and purity, researchers should document concentration, reconstitution solvent, buffer composition, temperature, incubation time, and any monomerization or pre-aggregation procedure. These parameters often have direct experimental significance.
Research Use Only.