Purity ~90% (SDS-PAGE). Prolyl Oligopeptidase, also known as prolyl endopeptidase and postproline cleaving enzyme, is a serine peptidase displaying specificity for the cleavage of ProXaa bonds of oligopeptide substrates (1, 2). The peptidase is known to hydrolyze a variety of biologically active peptides such as bradykinin, substance P, neurotensin, and vasopressin (3). Because of its action on neuropeptides, Prolyl Oligopeptidase is considered to be involved in processes such as learning, memory, and depression (4). Source: Recombinant corresponding to Leu2-Gln710 from mouse Prolyl Oligopeptidase/PREP, N-terminal Met, and 6-His tag, expressed in Spodoptera frugiperda, Sf 21 (baculovirus). Molecular Weight: ~82kD Biological Activity: Measured by its ability to convert the substrate benzyloxycarbonyl-Gly-Pro-7-amido- 4-methylcoumarin (Z-GP-AMC) to Z-Gly-Pro and 7-amino-4methylcoumarin (AMC). The specific activity is > 4,500 pmoles/min/ug, as measured under the described conditions. End