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Amyloid Beta 1-42 | CAS 107761-42-2

Beta-Amyloid (1-42) HFIP treated US$620.10 Excluding tax and shipping fees Limited stock Description About 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 prot

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Beta-Amyloid (1-42) HFIP treated

US$620.10

Excluding tax and shipping fees

Limited stock

Description

About 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, Swiss-Prot ID: P05067) 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: 2-5 days

Visit our webpage for more Peptide Tools to Study Alzheimer's Disease

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:

High neurotoxicity (suitable for toxicity assays) and strong relevance to Alzheimer’s pathology

Lower physiological abundance than Beta amyloid (1-40) (≈10-20% of total Aβ)

Rapid aggregation kinetics enabling robust oligomer and fibril generation

Poor solubility and rapid aggregation complicate handling

Dominant driver of early plaque formation and seeding

Strongly condition-dependent (buffer, pH, temperature)

Suitable for Aβ (1-42)/Aβ (1-40) biomarker ratio studies.

Sensitive to buffer, pH, and temperature.

Strong diagnostic relevance through reduced CSF Amyloid beta 1-42 levels and Aβ (1-42)/Aβ (1-40) ratio

Physiological function not fully understood

Relevant for familial AD models and monoclonal antibody-based therapeutics

Structural polymorphism and fast fibrillization reduce reproducibility and increase experimental variability

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

References

References for Beta-Amyloid (1-42) HFIP treated

References:Read References with Amyloid Beta A4 Peptides (abeta, aß)

Application Note Synthetic Amyloid Beta Peptides Aid Alzheimer Investigation Broersen et al., Application Note (2013) (full text)

Testimonial“Our group focuses on the in vitro study of risk factors in Alzheimer’s disease and, as we experienced that the in-house expression and production of the amyloid beta peptide is notoriously difficult, we are continuously dependent on a high quality supply of a large variety of these peptides from commercial source. We started our collaboration with JPT with their request to test a range of their peptides for the ability to produce toxic oligomers and fibrillar networks and were impressed by the rapid supply of a very wide range of high purity peptides with excellent fibril forming properties and toxicity profiles. JPT has shown real valuable know-how and experience in the field of peptide synthesis by their ability to generate high quality preparations of amyloid beta peptide variants which are known for their difficulty to handle.”Kerensa Broersen, Assistant Prof., Nanobiophysics Group, University of Twente, Enschede, The Netherlands

Documentation

Documentation for Beta-Amyloid (1-42) HFIP treated

Beta-Amyloid-1-42-HFIP-treated_0.5.pdf

Properties

Properties of Beta-Amyloid (1-42) HFIP treated

Abeta Peptides

Alzheimer's disease

Freeze-dried in plastic vial

Human

Amyloid beta (A4) protein

>95% (HPLC-MS)

No

Further Information to Beta-Amyloid (1-42) HFIP treated

Values

DAEFRHDSGYEVHHQKLVFFAEDVGSNKGAIIGLMVGGVVIA

Synthetic Beta-Amyloid peptide (1-42)

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Connected reading

Helpful context for this guide

Source-derived material selected through this article’s indexed topics.

Related questions

01What Drives MK-6240 Performance?

The performance of MK-6240 appears to be driven largely by differences in biologic binding characteristics, said Pascoal, who is also a behavioral neurologist at the University of Pittsburgh School of Medicine. “The main driver is biological affinity: MK-6240 binds tau tangles with roughly sixfold higher affinity than flortaucipir, as demonstrated in post-mortem tissue,” he explained. “This translates into a stronger signal-to-noise ratio in vivo, allowing detection of the sparse, early tangle deposits in medial temporal regions that flortaucipir tends to miss.” However, access to this newer tau PET tracer remains limited, he acknowledged. “Availability remains a real barrier,” Pascoal said. “MK-6240 is currently produced at a limited number of academic and trial-affiliated PET centers and is not yet approved as a routine clinical test.” The new agent received FDA Fast Track designation in 2025. The agency is expected to issue a decision on the manufacturer Lantheus’ new drug application expected in August, the company reported in a statement . The study provides evidence supporting sensitive approaches to tau detection, said Stephen Salloway, MD, director of Neurology and the Memory and Aging Program at Butler Hospital in Providence, Rhode Island, who was not part of the research. “Early detection of AD pathology will be critical for testing new interventions to slow or prevent cognitive decline in individuals at risk for AD,” and MK-6240 is better at detecting early stages of tau pathology than the currently available tracer, Salloway told Medscape Medical News . However, he cautioned that broader clinical implementation will require additional work to standardize interpretation and staging. “Better molecular staging of AD is needed to improve diagnostic accuracy and to identify individuals most likely to benefit from treatment,” he said. “Nuclear medicine specialists, radiologists, and dementia experts need experience and training to interpret tau PET scans.” The study was funded by the National Institute on Aging. Disclosure information for study authors is available in the original study publication. Salloway reported having no relevant financial disclosures.

Source: www.medscape.com ↗
Research context

Read sources and limitations before applying a claim.

What This Means for Researchers

This convergence of immunology and neuroscience is one of the most exciting fields of study right now. The similarities between LL-37 and Aβ open up entirely new avenues for therapeutic development and a deeper understanding of disease. Could we learn how to control pathological Aβ aggregation by studying how the body successfully regulates LL-37? Could modulating LL-37 levels or its activity be a novel therapeutic strategy for neuroinflammatory diseases? Answering these questions is a formidable challenge. It demands research materials of the highest possible quality. When you're investigating the subtle, concentration-dependent interactions between two peptides that can both help and harm, you simply cannot afford to have impurities or incorrect sequences in your samples. A tiny contaminant could skew aggregation kinetics or trigger an unintended inflammatory response, sending an entire research project down the wrong path. It's a difficult, often moving-target objective. That's the entire reason Real Peptides exists. Our commitment to small-batch synthesis and rigorous quality control ensures that the LL-37 and other compounds researchers use are exactly what they're supposed to be—pure, consistent, and reliable. This level of precision is a non-negotiable element for anyone working on the cutting edge. Our experience shows that breakthroughs are built on a foundation of trustworthy data, which starts with trustworthy reagents. This dedication to quality is something we apply across our full range of peptides. If your lab is ready to explore these complex biological questions, we're here to provide the high-purity tools you need to find clear answers. You can [Get Started Today] and see the difference that uncompromising quality makes. The story of LL-37 and Aβ is a potent reminder that biology doesn't operate in neat silos. The systems that protect us from microbes are deeply intertwined with the processes that can lead to chronic disease and aging. The villain may be a hero in a different context, and the hero's power, left unchecked, can cause its own form of damage. By understanding their surprising similarities, we're not just learning about two peptides; we're gaining a more profound insight into the delicate and often paradoxical nature of life itself.

Source: realpeptides.co ↗
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