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A2T-Beta-Amyloid (1-42) HFIP treated peptide (0.5 mg)

A2T-Beta-Amyloid (1-42) HFIP treated US$620.10 Excluding tax and shipping fees Currently out of stock, available again soon Description About A2T-Beta-Amyloid (1-42) HFIP treated Synthetic peptide derived from the N-terminal region of human Amyloid beta A4 pro

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A2T-Beta-Amyloid (1-42) HFIP treated

US$620.10

Excluding tax and shipping fees

Currently out of stock, available again soon

Description

About A2T-Beta-Amyloid (1-42) HFIP treated

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.

A2T-Beta-Amyloid (1-42) HFIP treated - Specifications

Purity: >95% (HPLC-MS)

Delivery Format: Freeze-dried in plastic vial

Application(s):

Condition(s)/Topic(s): Alzheimer's disease

Standard Delivery Time: approx. 3 weeks

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

Are you interested in your other Abeta Peptides? Choose your sequence, amount and purity. We will assist you along the way. Custom Peptide Synthesis.

JPT's Single Catalog Peptides 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 A2T-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 A2T-Beta-Amyloid (1-42) HFIP treated

A2T-Beta-Amyloid-1-42-HFIP-treated_0.5.pdf

Properties

Properties of A2T-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 A2T-Beta-Amyloid (1-42) HFIP treated

Values

DTEFRHDSGYEVHHQKLVFFAEDVGSNKGAIIGLMVGGVVIA

Point mutated 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.

Research context

Read sources and limitations before applying a claim.

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).

Source: jpt.com ↗
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