Beta-Amyloid 1-42 HFIP treated

Beta-amyloid (1-42), also known as Aβ (1-42), is a 42-amino acid peptide generated from the human amyloid precursor protein (APP) and is thought to contribute to neuronal function. When its clearance is impaired, the peptide rapidly aggregates into β-sheet-rich oligomers and fibrils that initiate amyloid plaque formation and promote neuronal damage. Known as the more aggregation-prone isoform, this peptide is strongly linked to Alzheimer’s disease and widely used in neurodegenerative research to study rapid aggregation events, neurotoxicity, and early plaque formation.

HFIP treatment breaks down pre-formed aggregates and returns Amyloid beta 1 42 peptides to a monomeric state, ensuring a reproducible and clean starting material for experiments. For research use only, do not use in humans!

Produced by JPT Peptide Technologies, a leader in custom peptide synthesis for Alzheimer’s research.

Synthetic peptide derived from the N-terminal region of human Amyloid beta A4 protein (Swiss-Prot ID: P05067). HFIP treatment is performed to disrupt beta-sheets and other unwanted secondary structures.

Beta-Amyloid 1-42 HFIP treated - Specifications

• Purity: >95% (HPLC-MS)
• Delivery Format: Freeze-dried in plastic vial
• CAS: 107761-42-2
• Application(s):
• Condition(s)/Topic(s): Alzheimer's disease
• Standard Delivery Time: approx. 3 weeks

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Research areas and applications of Beta-Amyloid (1-42), CAS: 107761-42-2

• Neurodegeneration and Alzheimer’s research: Used to study how Amyloid beta 1-42 overproduction, impaired clearance, and rapid aggregation drive Alzheimer’s progression due to its high neurotoxicity and strong synaptic impact.
• Amyloid aggregation and plaque formation studies: Serves as a model for fast β-sheet nucleation, toxic oligomer formation, and the development of protofibrils and mature fibrils using NMR, AFM, and cryo-EM.
• Neurotoxicity, synaptic physiology, and neuronal function: Used to examine how beta amyloid oligomers disrupt synaptic signaling, alter calcium balance, impair plasticity, induce oxidative stress, and activate apoptosis that contributes to neuronal dysfunction.
• Anti-amyloid drug discovery and therapeutic development: Utilized to screen aggregation inhibitors, test Aβ-targeting monoclonal antibodies (e.g., beta amyloid 1-42 antibody), evaluate peptide-based therapeutics, and model compound effects that reduce amyloid burden.
• Biomarker development and diagnostics: Supports CSF and blood biomarker studies focused on decreased peptide levels and its ratio with Amyloid beta (1-40), both strongly linked to amyloid PET imaging and early Alzheimer’s diagnosis.
• APP processing and familial Alzheimer’s disease research: Used to analyze how APP, PSEN1, and PSEN2 mutations shift γ-secretase cleavage toward increased Amyloid beta (1-42), modeling mechanisms of familial Alzheimer’s disease.
• Neuroinflammation research: Applied to study microglial and astrocytic activation, cytokine release, and inflammatory responses induced by Amyloid beta aggregates that stimulate innate immune pathways.
• Seeding and cross-seeding studies: Used to examine how it acts as a nucleation seed for Aβ (1-40) fibrillization and how mixed Aβ species form distinct fibril structures in plaques.
• Comparison studies with Aβ (1-40): Used to compare aggregation kinetics, toxicity, structural stability, and diagnostic relevance with Beta amyloid (1-40).

Benefits and limitations

A brief overview of the peptide’s strengths and limitations in experimental studies is shown below:

Key Concepts

What is a HFIP treatment?

Hexafluoroisopropanol (HFIP) is a strongly fluorinated solvent widely used in peptide research because it disrupts hydrogen bonds and can solubilize peptide assemblies that are otherwise difficult to dissolve. In studies involving amyloid beta, HFIP is used to break apart existing fibrils and oligomers by interfering with their beta sheet structures. This treatment returns the Abeta peptides to their monomeric forms and ensures a consistent, well defined starting point for controlled experimental work.

JPT's Single Catalog Peptides
Beta Amyloid (1-42) belongs to our Single Catalog Peptides and is manufactured according to the same high-quality standards applied across our peptide catalog. JPT Peptide Technologies has substantial, long-standing expertise in providing peptides, peptidomimetics, and proteins to the global scientific community. Our highly skilled and committed scientific staff ensures that the most appropriate methods and techniques are selected for every synthesis project. All of JPT's catalog peptides are provided with HPLC-MS analyses to confirm the identity and demonstrate the high quality of our peptides.

Benefits of JPT's Single Catalog Peptides
- Synthesis protocols designed to avoid toxic contaminants and side products
- Provision of freeze dried aliquots for enhanced stability
- Proven track record for applications in clinical studies