Amylin, human, free acid contains a free carboxyl terminus influencing charge distribution and solubility. The peptide is applied in studies of aggregation mechanisms, β-structure formation, and membrane interaction. Its amphipathic features support folding and structural analyses. Research areas include amyloid biophysics and peptide engineering.
CAT No: A12014
1. Cell-based adhesion assays for isolation of snake venom’s integrin antagonists
3. Adipose tissue is a key organ for the beneficial effects of GLP-2 metabolic function
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