Pfu Aminopeptidase I

Edman degradation is a commonly used method for protein sequencing via N-terminal amino acid cleavage. Pfu Aminopeptidase I is a thermostable exo-type aminopeptidase isolated from Pyrococcus furiosus. It is expressed as a recombinant protein and liberates N-terminal amino acids from proteins and peptides. While Pfu Aminopeptidase I has a wide range of substrate specificities, it does not hydrolyze peptide bonds at the α-amino group of proline (X-Pro). Enzyme activity is significantly increased in the presence of Co2+. Pfu Aminopeptidase I is a thermostable exo-type aminopeptidase isolated from Pyrococcus furiosus. It is produced as a recombinant protein, which liberates the N-terminal amino acid from proteins and peptides. This enzyme has a wide range of substrate specificity, and it does not hydrolyze peptide bonds at the α-amino residue side of proline (X-Pro). It is significantly activated in the presence of a Co2+ ion. Our products are to be used for Research Use Only. They may not be used for any other purpose, including, but not limited to, use in humans, therapeutic or diagnostic use, or commercial use of any kind. Our products may not be transferred to third parties, resold, modified for resale, or used to manufacture commercial products or to provide a service to third parties without our prior written approval. Recombinant Escherichia coli encoding the Pyrococcus furiosus aminopeptidase I gene One unit of enzyme activity corresponds to the amount required to hydrolyze 1 µmol of Leucine-p-nitroanilide at 75°C, pH 8.0 in one minute.