Renin Inhibitor III employs a peptide framework optimized to occupy renin's active-site cleft, enabling precise structure-activity evaluation. Its residue pattern is designed for high-affinity interaction in biochemical assays. The sequence supports mechanistic analyses of substrate mimicry. Researchers apply it in kinetic profiling, inhibitor characterization, and active-site modeling.
CAT No: R01024
1. Implications of ligand-receptor binding kinetics on GLP-1R signalling
2. Peptides as Active Ingredients: A Challenge for Cosmeceutical Industry
5. The spatiotemporal control of signalling and trafficking of the GLP-1R
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