Peptidases and proteases are important components of cell regulation and signaling, protein activation and synthesis, and other metabolic pathways. Proteases generally cleave longer proteins, while peptidases cleave shorter peptide bonds. Peptidases are further subdivided depending on their hydrolysis sites: endopeptidases cleave internal peptide bonds while exopeptidases hydrolyze terminus residues. 1. Specific amine-containing fluorophores can be conjugated to amino acids and/or proteins through the carboxy terminus, producing fluorogenic peptidase substrates with shorter or non-detectable emission spectra. Upon peptidase activity, the fluorophore is released and the fluorescence restored. 2. Substrate suitability generally depends on enzyme accessibility and the permeability of the substrate and its hydrolyis product.
Sensitive fluorogenic substrate for leucine aminopeptidase and aminopeptidase M detection which releases the bright blue fluorescent dye, 7-amino-4-methylcoumarin M1059 upon enzyme activity with emission 440nm upon at excitation 380nm. Learn More