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15N-Beta-Amyloid (1-42), Uniformly Labeled, Human, Recombinant

Sequence: DAEFRHDSGY EVHHQKLVFF AEDVGSNKGA IIGLMVGGVV IA

           
Product Catalog # SizePrice (USD) Quantity
$100.00
$300.00
$450.00
$2,000.00
Synonym: 15N Stable Isotope Labeled Beta-Amyloid (1-42); 15N-β-Amyloid (1-42); 15N-Aβ (1-42)
Unlabeled CAS #: 107761-42-2
UniProt ID: P05067
Source: E. coli
Molecular Formula: C203H311(15N)55O60S
Molecular Weight: 4569.1
Uniformly 15N isotope-labeled β-amyloid (Aβ1-42) is an essential stable isotope-labeled peptide reagent widely used in Alzheimer’s disease research, structural biology, and biophysical studies of amyloid aggregation. The incorporation of the nitrogen-15 isotope enables advanced heteronuclear NMR analyses while maintaining the native biochemical properties of Aβ1-42. Because Aβ1-42 is the predominant amyloid species associated with plaque formation and exhibits higher aggregation propensity than Aβ1-40, uniformly 15N-labeled Aβ1-42 provides a powerful platform for investigating early oligomer formation, fibril assembly, membrane interactions, and therapeutic intervention strategies.
1. Introduction
β-Amyloid peptides are generated through proteolytic processing of the amyloid precursor protein (APP). Among the major isoforms, Aβ(1-42) is considered one of the most pathogenic forms due to its strong tendency to self-assemble into soluble oligomers and insoluble amyloid fibrils.
Compared with Aβ(1-40), the additional two C-terminal residues (Ile41 and Ala42) significantly increase hydrophobicity, β-sheet formation, and aggregation kinetics. These properties make Aβ1-42 a primary target for studying the molecular mechanisms underlying Alzheimer’s disease (AD).
2. Importance of 15N Isotope Labeling
Uniform incorporation of 15N throughout the peptide backbone provides several important advantages:
• Enables high-resolution 1H–15N HSQC NMR spectroscopy.
• Allows residue-specific monitoring of conformational changes during aggregation.
• Facilitates backbone resonance assignments and structural characterization.
• Enables kinetic studies of oligomerization and fibril formation.
• Supports interaction studies with membranes, metal ions, antibodies, and small-molecule inhibitors.
• Provides enhanced analytical capability without altering peptide function because 15N is a stable, non-radioactive isotope.
The mass increase caused by 15N substitution is minimal and does not significantly influence peptide folding, aggregation, or biological activity.
3. Major Research Applications
Uniformly 15N-labeled Aβ1-42 is commonly applied in:
3.1. Amyloid Aggregation Studies
Aβ1-42 aggregation involves multiple transient intermediates, including soluble oligomers and protofibrils. Isotope-edited NMR techniques allow researchers to monitor residue-specific structural transitions during these processes.
3.2 Structural Biology
15N-labeled Aβ1-42 is used for:
• Solution NMR analysis of monomeric and oligomeric species
• Solid-state NMR studies of fibril structures
• Mapping conformational dynamics
• Investigating intermolecular β-sheet formation
3.3 Membrane Interaction Studies
Aβ1-42 toxicity is closely associated with interactions with neuronal membranes. 15N labeling enables characterization of peptide binding, insertion, and structural changes upon interaction with:
• Lipid bilayers
• Cholesterol-containing membranes
• Model neuronal membranes
3.4 Drug Discovery and Therapeutic Development
The peptide is widely used for evaluating:
• Amyloid aggregation inhibitors
• Anti-amyloid antibodies
• Small-molecule modulators
• Peptide-based therapeutic approaches
4. Structural Characteristics
NMR and complementary structural studies have demonstrated that monomeric Aβ1-42 is highly flexible and intrinsically disordered in solution. During aggregation, it undergoes conformational transitions leading to β-sheet-rich structures.
Important structural regions include:
• Residues 17-21 (LVFFA): hydrophobic core involved in aggregation initiation
• C-terminal residues 30-42: critical for fibril stability and increased aggregation tendency
• N-terminal region (1-16): involved in metal binding, antibody recognition, and intermolecular interactions
The unique aggregation behavior of Aβ1-42 makes it an important model for studying early pathological events in AD.
5. Future Perspectives
Uniformly 15N-labeled Aβ1-42 continues to support emerging research areas, including:
• Structural characterization of toxic oligomer intermediates
• In-cell and membrane-associated amyloid studies
• NMR-guided drug discovery
• Integration with cryo-electron microscopy (cryo-EM)
Uniformly 15N-labeled β-amyloid (1-42) is a valuable research tool for understanding the molecular mechanisms of Alzheimer’s disease. Its enhanced compatibility with multidimensional NMR techniques enables detailed investigation of amyloid conformational dynamics, aggregation pathways, and molecular interactions. Due to the critical role of Aβ1-42 in amyloid pathology, 15N-labeled Aβ1-42 remains an important reagent for neuroscience research, biomolecular structural studies, and therapeutic development.

For Research & Development use only. Not for testing and/or use on humans.

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