Beta-Amyloid (12-42) extends from the central domain through the C-terminal hydrophobic segment, forming a robust model of fibril formation. The peptide displays rapid β-sheet development and aggregation in controlled environments. Its length permits investigation of protofibril stability and intermolecular packing. Researchers employ it in structural biology, aggregation-modulator evaluation, and supramolecular modeling.
CAT No: A13200
2. Implications of ligand-receptor binding kinetics on GLP-1R signalling
4. An Open-label, Single-center, Safety and Efficacy Study of Eyelash Polygrowth Factor Serum
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