Phe-Pro-Arg-PABA-Resorufin is a Chromogenic and fluorogenic peptide substrate for the highly sensitive detection of proteases in biological matrices. The substrate is also applicable to the sensitive detection of the thrombin inhibitor dabigatran in human
Phe-Met-Arg-Phe, amide dose-dependently (ED50=23 nM) activates a K+ current in peptidergic caudodorsal neurons and appears to localize with neuropeptide Y in some brain regions.
H-D-Phe-Pip-Arg-pNA (S-2238) acetate is a chromogenic substrate designed based on the N-terminal fragment of the A alpha chain of fibrinogen, which is the physiological target of thrombin. As a specific indicator of thrombin activity, H-D-Phe-Pip-Arg-pNA acetate is utilized to quantify. This assay, utilizing H-D-Phe-Pip-Arg-pNA acetate, ensures high sensitivity, accuracy, and ease of execution.
pGlu-Pro-Arg-MNA monoacetate, a thrombin substrate modeled after a thrombin cleavage site in human fibrinogen, can be used for sensitive assays of antithrombin III activity.
Tos-Gly-Pro-Arg-ANBA-IPA, a chromogenic peptide substrate, is utilized for the rapid and specific photometric assay of recombinant hirudin (r-hirudin).
Pro-Phe-Phe, a highly aggregation-prone tripeptide composed of natural amino acids, exhibits the formation of distinctive helical-like sheets that engage in aromatic dry interfaces. This property makes Pro-Phe-Phe an excellent candidate for the development of modular super-helical self-assembling nanostructures.
Phe-Met-Arg-Phe-like peptide, derived from the visceral and somatic muscles of the snail Helix aspersa, is a neuropeptide known as FMRF (Phe-Met-Arg-Phe). This peptide comprises four amino acid residues[1].