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15N-Beta-Amyloid (1-40), Uniformly Labeled, Human, Recombinant

Sequence: DAEFRHDSGY EVHHQKLVFF AEDVGSNKGA IIGLMVGGVV

           
Product Catalog # SizePrice (USD) Quantity
$100.00
$300.00
$450.00
$2,000.00
Synonym: 15N Stable Isotope Labeled Beta-Amyloid (1-40); 15N-β-Amyloid (1-40); 15N-Aβ (1-40)
Unlabeled CAS #: 131438-79-4
UniProt ID: P05067
Source: E. coli
Molecular Formula: C194H295(15N)53O58S
Molecular Weight: 4382.8
Uniformly 15N isotope-labeled β-amyloid (Aβ1-40) is one of the most widely used reagents for structural and biophysical investigations of Alzheimer’s Disease (AD). Incorporation of the stable nitrogen-15 isotope into every nitrogen-containing atom of the peptide enables high-resolution heteronuclear nuclear magnetic resonance (NMR) spectroscopy without altering the peptide’s native physicochemical or biological properties. Compared with unlabeled Aβ(1-40), the 15N-labeled analog exhibits identical aggregation behavior, fibril morphology, and neurotoxicity while providing greatly enhanced spectral resolution and sensitivity in multidimensional NMR experiments. Consequently, uniformly 15N-labeled Aβ(1-40) has become an indispensable tool for elucidating amyloid folding pathways, aggregation mechanisms, membrane interactions, and the effects of therapeutic inhibitors.
1. Introduction
β-Amyloid (Aβ) peptides are generated by sequential cleavage of the amyloid precursor protein (APP) by β- and γ-secretases. Among the naturally occurring isoforms, Aβ(1-40) accounts for approximately 90% of soluble Aβ species produced in the human brain, whereas Aβ(1-42) is more aggregation-prone and neurotoxic.
Although Aβ(1-40) aggregates more slowly than Aβ(1-42), it serves as an excellent model system for investigating amyloid formation because its aggregation kinetics are experimentally more manageable and highly reproducible.
2. Advantages of Uniform 15N Labeling
Uniform incorporation of 15N into Aβ(1-40) offers several significant advantages:
• Enables two-dimensional 1H-15N HSQC experiments with excellent spectral dispersion.
• Allows complete backbone resonance assignments using triple-resonance NMR.
• Facilitates residue-specific investigation of conformational changes during aggregation.
• Permits quantitative measurements of molecular dynamics and exchange processes.
• Supports isotope-filtered experiments for studying interactions with membranes, metal ions, antibodies, and small-molecule inhibitors.
• Produces no measurable perturbation of peptide folding or aggregation because 15N is a stable, non-radioactive isotope.
3. Major Applications
Uniformly 15N-labeled Aβ(1-40) is extensively used in:
• Solution-state NMR studies of monomeric Aβ
• Solid-state NMR characterization of amyloid fibrils
• Aggregation kinetics and nucleation studies
• Structural determination of oligomeric intermediates
• Internal mass spectrometry standard and general biomarker reference reagent
• Membrane interaction studies
• Drug discovery and inhibitor screening
• Mechanistic studies of metal-ion binding (Cu2+, Zn2+, Fe3+)
• Molecular dynamics validation and computational modeling
4. Structural Insights
NMR studies using uniformly 15N-labeled Aβ(1-40) have revealed several important structural features:
• Freshly dissolved monomeric Aβ(1-40) is largely intrinsically disordered.
• Early oligomerization induces transient β-sheet formation.
• Mature fibrils adopt the characteristic cross-β amyloid architecture.
• The central hydrophobic region (residues 17-21) and C-terminal segment play dominant roles in fibril stabilization.
• Residue-specific chemical shift changes identify transient conformational intermediates during aggregation.
These discoveries have greatly advanced understanding of amyloid self-assembly and Alzheimer’s disease pathology.
5. Future Perspectives
Uniformly 15N-labeled Aβ(1-40) continues to play a central role in Alzheimer’s disease research. Emerging applications include:
• Cryo-EM/NMR hybrid structural analyses
• In-cell NMR investigations
• Studies of liquid–liquid phase separation
• Screening of aggregation inhibitors
• Development of isotope-edited multidimensional spectroscopy methods
Uniformly 15N-labeled β-amyloid (1-40) has become a cornerstone reagent in amyloid structural biology. By enabling residue-specific structural and dynamic characterization while preserving the peptide’s native behavior, it provides unparalleled insight into the molecular mechanisms underlying amyloid aggregation and Alzheimer’s disease. Continued advances in isotope-labeling technologies and high-resolution spectroscopic methods will further expand its value in mechanistic studies and therapeutic development.

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

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