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Beta-Amyloid (1-40) HFIP treated peptide (0.5 mg)

Beta-Amyloid (1-40) HFIP treated US$577.20 Excluding tax and shipping fees Limited stock Description About Beta-Amyloid (1-40) HFIP treated Beta-Amyloid (1-40), also known as Abeta (1-40), is a 40-amino-acid peptide derived from the human amyloid precursor pro

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Beta-Amyloid (1-40) HFIP treated

US$577.20

Excluding tax and shipping fees

Limited stock

Description

About Beta-Amyloid (1-40) HFIP treated

Beta-Amyloid (1-40), also known as Abeta (1-40), is a 40-amino-acid peptide derived from the human amyloid precursor protein (APP). It corresponds to the predominant amyloid-β isoform in the brain, presumed to support neuronal function. When its clearance is impaired, it can aggregate into β-sheet-rich oligomers and fibrils, which contribute to amyloid plaque formation and cause neuronal damage. The peptide is therefore closely linked to Alzheimer’s disease and widely used in neurodegenerative research to study amyloid aggregation, plaque formation, and neurotoxicity.

HFIP breaks down pre-formed aggregates and returns beta amyloid (1-40) peptides (CAS: 131438-79-4) to a monomeric state, ensuring a clean, reproducible 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 (1-40) HFIP treated - Specifications

Purity: >95% (HPLC-MS)

Delivery Format: Freeze-dried in plastic vial

CAS: 131438-79-4

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

Role of Beta amyloid (1-40) in Alzheimer’s disease?

Beta amyloid (1-40) is one of the main peptides produced when the amyloid precursor protein (APP) is cleaved by β- and γ-secretases. It is the most abundant soluble form of amyloid beta peptides in the brain and is found at higher levels than Aβ (1-42). Although Amyloid beta 1-40 aggregates more slowly, it plays an important regulatory role in Alzheimer’s disease by interacting with Aβ (1-42), shaping fibril structure, and influencing plaque stability and toxicity.

Impaired production or clearance of Amyloid beta (1-40) also contributes to vascular amyloid deposition (cerebral amyloid angiopathy), making it a key component of the broader amyloid cascade linked to Alzheimer’s pathology.

Visit our webpage to learn more about Alzheimer’s Disease and Amyloid Beta Peptides!

Research areas and applications of Beta Amyloid (1-40):

Neurodegeneration and Alzheimer’s research: Used to investigate how Beta amyloid (1-40) production, clearance, and aggregation contribute to Alzheimer’s or other neurodegenerative diseases like dementia.

Amyloid aggregation and plaque formation studies: Serves as a model for studying β-sheet formation and the progression from oligomers to protofibrils and mature fibrils using structural techniques such as NMR, AFM, and cryo-EM.

Mechanisms of neurotoxicity: Employed to analyze how soluble oligomers disrupt synaptic signaling, induce oxidative stress, trigger apoptosis, and impair neuronal membrane integrity.

Cerebrovascular research: Used to study the impact of 40-amino-acid beta amyloid isoform on cerebral blood vessels, including vascular dysfunction, impaired blood-flow regulation, and mechanisms underlying cerebral amyloid angiopathy (CAA).

Neuroinflammation research: Applied in studies exploring microglial activation, cytokine release, and inflammatory responses triggered by aggregated beta amyloid species.

Biomarker development and diagnostics: Supports the development of CSF and blood biomarkers (e.g., Aβ (1-42)/Aβ (1-40) ratio) that strongly correlate with amyloid PET imaging, providing an indirect link to PET-based Alzheimer’s diagnosis.

Anti-amyloid drug discovery and therapeutic development: Utilized to screen inhibitors of aggregation, test monoclonal antibodies targeting Aβ peptides, evaluate peptide-based therapeutics, and model the effects of candidate compounds that reduce toxicity or promote clearance.

Systemic health research: Employed in studies investigating links between circulating Amyloid-beta (1-40) levels and systemic disorders such as kidney dysfunction and cardiovascular diseases.

Physiological function studies: Used to examine potential normal roles of low-level Beta-amyloid (1-40) in synaptic regulation, neural development, and antioxidant activity.

Comparison studies with Amyloid beta (1-42): Used in comparison studies with Amyloid beta (1-42) to evaluate differences in concentration, aggregation behavior, and diagnostic value in Alzheimer’s research.

Benefits and limitations:

A brief overview of the strengths and limitations of Abeta (1-40) in experimental studies is shown below:

High physiological abundance in brain and CSF (≈80-90% of total Aβ).

Lower neurotoxicity and weaker amyloid-forming tendency than Aβ (1-42).

Better solubility and handling than Aβ (1-42).

Less relevant to early plaque formation; Aβ (1-42) dominates early deposition.

Slower aggregation behavior than Aβ (1-42).

Levels show weak correlation with plaque burden.

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

Sensitive to buffer, pH, and temperature.

Useful for early in vitro aggregation and kinetics research.

Forms mixed species (monomers, oligomers, protofibrils).

Distinct fibril morphology valuable for comparative studies.

Physiological function not fully understood.

Key Concepts

What is a HFIP treatment?

Hexafluoroisopropanol (HFIP) is a highly fluorinated organic solvent commonly used in peptide research because it can disrupt hydrogen bonding and dissolve otherwise stable peptide aggregates. In amyloid-beta studies, HFIP treatment breaks down pre-formed fibrils or oligomers by disrupting their β-sheet structures. This process restores amyloid beta peptides to a monomeric state, providing reproducible and well-defined starting material for controlled experiments.

JPT's Single Catalog Peptides Beta Amyloid 1-40 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 (1-40) 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 (1-40) HFIP treated

Beta-Amyloid-1-40-HFIP-treated_0.5.pdf

Properties

Properties of Beta-Amyloid (1-40) 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 (1-40) HFIP treated

Values

DAEFRHDSGYEVHHQKLVFFAEDVGSNKGAIIGLMVGGVV

Synthetic Beta-Amyloid peptide (1-40)

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Research context

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Research areas and applications:

Alzheimer’s and neurodegenerative research: Used as a defined model of early Beta-amyloid (1-40) oligomers to study initial pathogenic events in Alzheimer’s disease and related neurodegenerative conditions. Amyloid aggregation and plaque formation studies: Provides a controlled starting point for tracking the conversion of dimers into higher-order oligomers and protofibrils using structural techniques such as NMR, AFM, and TEM. Early neurotoxicity and synaptic dysfunction studies: Enables analysis of how stabilized amyloid beta dimers disrupt synaptic signaling, impair membranes, induce oxidative stress, and contribute to neuronal dysfunction. Memory and LTP impairment studies: Applied in neuronal and animal models to investigate how amyloid beta dimers impair long-term potentiation and drive early cognitive decline. Seeding and propagation research: Used to examine how defined amyloid beta dimers act as seeds that accelerate aggregation or influence amyloid propagation behavior. Protein-peptide, receptor, and membrane interactions: Applied to study how early the 40-amino-acid long amyloid beta oligomers bind to lipid bilayers, neuronal receptors (e.g., PrP), and other membrane components involved in amyloid beta toxicity. Anti-amyloid drug discovery and therapeutic development: Utilized for screening aggregation inhibitors, testing monoclonal antibodies, and evaluating small molecules targeting early oligomer formation or toxicity. Structure-function analyses: Supports detailed studies of dimer structure, stability, and conformational changes, linking specific structural features to downstream toxicity. Comparative studies: Enables direct comparison with monomeric amyloid beta peptides to assess differences in aggregation, toxicity, and oligomer behavior.

Source: jpt.com ↗
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Peptide Therapy Guide Editorial Team

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