Beta-Amyloid (20-42) – 1 mg

Overview

Beta-Amyloid (20-42) is a synthetic peptide that corresponds to amino acids 20 to 42 of the amyloid-beta protein, which is critical in neuroscience research, especially in studies related to Alzheimer’s disease. With its specific sequence, this peptide allows for accurate modeling and analysis of amyloid-beta’s role in neurodegenerative processes. This makes it an essential tool for researchers aiming to unravel the complexities of neurological disorders. You can also explore our full range of peptides to find other relevant products that may assist your studies.

Key Features

• High purity synthetic peptide, ensuring reliable results in experimental procedures.
• Specific sequence enables targeted research on amyloid-beta aggregation.
• Ideal for applications in drug discovery and therapeutic development.
• Manufactured under strict quality controls to meet research standards.
• Available in a convenient 1 mg package, perfect for smaller research projects.

Specifications

FAQ

What applications is Beta-Amyloid (20-42) used for?

This peptide is primarily used in research related to Alzheimer’s disease and other neurodegenerative disorders. It aids in studying amyloid plaque formation, cellular toxicity, and potential therapeutic targets.

How should I store this peptide?

Beta-Amyloid (20-42) should be stored at -20°C or lower. It is recommended to keep it in a dry, cool place, away from direct sunlight to maintain its stability and efficacy.

Can this peptide be used in vivo?

While Beta-Amyloid (20-42) is typically used in vitro for various assays and studies, further evaluation and appropriate formulations are necessary for in vivo applications. Researchers should conduct initial safety assessments before utilizing it in living subjects.

For further research projects involving substrates, consider exploring our PKG substrate options or diving into more specific peptide sequences like Autocamtide-2. Order Beta-Amyloid (20-42) today to enhance your research on Alzheimer’s disease and neurobiology.

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