Recombinant Human Prolyl Oligopeptidase/PREP Protein, CF

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Product Details

Summary
Reactivity HuSpecies Glossary
Applications Enzyme Activity
Format
Carrier-Free

Order Details

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.
Source
Spodoptera frugiperda, Sf 21 (baculovirus)-derived human Prolyl Oligopeptidase/PREP protein
Leu2-Pro710, with an N-terminal Met and 6-His tag
Accession #
N-terminal Sequence
Met
Protein/Peptide Type
Recombinant Enzymes
Gene
PREP
Purity
>95%, by SDS-PAGE under reducing conditions and visualized by silver stain
Endotoxin Note
<1.0 EU per 1 μg of the protein by the LAL method.

Applications/Dilutions

Theoretical MW
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.
SDS-PAGE
73 kDa, reducing conditions
Publications
Read Publication using
4308-SE in the following applications:

Packaging, Storage & Formulations

Storage
Use a manual defrost freezer and avoid repeated freeze-thaw cycles.
  • 6 months from date of receipt, -20 to -70 °C as supplied.
  • 3 months, -20 to -70 °C under sterile conditions after opening.
Buffer
Supplied as a 0.2 μm filtered solution in MES, NaCl and Glycerol.
Purity
>95%, by SDS-PAGE under reducing conditions and visualized by silver stain
Assay Procedure
  • Assay Buffer: 25 mM Tris, 250 mM NaCl, 2.5 mM DTT, pH 7.5
  • Recombinant Human Prolyl Oligopeptidase/PREP (rhPREP) (Catalog # 4308-SE)
  • Substrate: Z-Gly-Pro-AMC (Bachem, Catalog # I-1145)
  • F16 Black Maxisorp Plate (Nunc, Catalog # 475515)
  • Fluorescent Plate Reader (Model: SpectraMax Gemini EM by Molecular Devices) or equivalent
  1. Dilute rhPREP to 0.1 µg/mL in Assay Buffer.
  2. Dilute Substrate to 100 µM in Assay Buffer.
  3. Incubate at room temperature for 5 minutes.
  4. 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.
  5. Read at excitation and emission wavelengths of 380 nm and 460 nm (top read), respectively, in kinetic mode for 5 minutes.
  6. 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).

Per Well:
  • rhPREP: 0.005 µg
  • Substrate: 50 µM

Notes

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)
  • EC 3.4.21.26
  • MGC16060
  • PE
  • PEP
  • Post-proline cleaving enzyme
  • PREP
  • prolyl endopeptidase
  • Prolyl Oligopeptidase
  • rPop

Background

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).

  1. Tarrago, T. et al. (2005) J. Pept. Sci. 11:283.
  2. Yoshimoto, T. et al. (1977) Biochemistry. 16:2942.
  3. Wilk, S. (1983) Life Sci. 33:2149.
  4. Maes, M. et al. (1994) Biol. Psychiatry. 35:545.

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Publications for Prolyl Oligopeptidase/PREP (4308-SE)(1)

We have publications tested in 1 confirmed species: Human.

We have publications tested in 1 application: EnzAct.


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EnzAct
(1)
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(1)
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Bioinformatics

Gene Symbol PREP
Entrez
Uniprot