Recombinant Human Prolyl Oligopeptidase/PREP Protein, CF Summary
Details of Functionality
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-4-methylcoumarin (AMC). The specific activity is >3,500 pmol/min/µg, as measured under the described conditions.
Spodoptera frugiperda, Sf 21 (baculovirus)-derived human Prolyl Oligopeptidase/PREP protein Leu2-Pro710, with an N-terminal Met and 6-His tag
>95%, by SDS-PAGE under reducing conditions and visualized by silver stain
<1.0 EU per 1 μg of the protein by the LAL method.
81 kDa. Disclaimer note: The observed molecular weight of the protein may vary from the listed predicted molecular weight due to post translational modifications, post translation cleavages, relative charges, and other experimental factors.
73 kDa, reducing conditions
Read Publication using 4308-SE in the following applications:
Fluorescent Plate Reader (Model: SpectraMax Gemini EM by Molecular Devices) or equivalent
Dilute rhPREP to 0.1 µg/mL in Assay Buffer.
Dilute Substrate to 100 µM in Assay Buffer.
Incubate at room temperature for 5 minutes.
Load 50 µL of 0.1 µg/mL of rhPREP into a plate, and start the reaction by adding 50 µL of 100 µM Substrate. Include a Substrate Blank containing 50 µL of Assay Buffer and 50 µL of Substrate.
Read at excitation and emission wavelengths of 380 nm and 460 nm (top read), respectively, in kinetic mode for 5 minutes.
Calculate specific activity:
Specific Activity (pmol/min/µg) =
Adjusted Vmax* (RFU/min) x Conversion Factor** (pmol/RFU)
amount of enzyme (µg)
*Adjusted for Substrate Blank **Derived using calibration standard 7-amino, 4-Methyl Coumarin (AMC) (Sigma, Catalog # A-9891).
rhPREP: 0.005 µg
Substrate: 50 µM
This product is produced by and ships from R&D Systems, Inc., a Bio-Techne brand.
Alternate Names for Recombinant Human Prolyl Oligopeptidase/PREP Protein, CF
dJ355L5.1 (prolyl endopeptidase)
Post-proline cleaving enzyme
Prolyl Oligopeptidase is a serine peptidase displaying specificity for the cleavage of Pro-Xaa 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).
Tarrago, T. et al. (2005) J. Pept. Sci. 11:283.
Yoshimoto, T. et al. (1977) Biochemistry. 16:2942.
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