Human Prolyl Oligopeptidase/PREP Antibody

Catalog # Availability Size / Price Qty
AF4308
AF4308-SP
Product Details
Citations (3)
FAQs
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Human Prolyl Oligopeptidase/PREP Antibody Summary

Species Reactivity
Human
Specificity
Detects human PREP in direct ELISAs and Western blots. In direct ELISAs, approximately 50% cross-reactivity with recombinant mouse PREP is observed.
Source
Polyclonal Goat IgG
Purification
Antigen Affinity-purified
Immunogen
S. frugiperda insect ovarian cell line Sf 21-derived recombinant human PREP
Leu2-Pro710
Accession # P48147
Formulation
Lyophilized from a 0.2 μm filtered solution in PBS with Trehalose. *Small pack size (SP) is supplied either lyophilized or as a 0.2 µm filtered solution in PBS.
Label
Unconjugated

Applications

Recommended Concentration
Sample
Western Blot
0.1 µg/mL
Recombinant Human Prolyl Oligopeptidase/PREP (Catalog # 4308-SE)
Immunoprecipitation
25 µg/mL
Cell lysates spiked with Recombinant Human Prolyl Oligopeptidase/PREP (Catalog # 4308‑SE), see our available Western blot detection antibodies

Please Note: Optimal dilutions should be determined by each laboratory for each application. General Protocols are available in the Technical Information section on our website.

Reconstitution Calculator

Reconstitution Calculator

The reconstitution calculator allows you to quickly calculate the volume of a reagent to reconstitute your vial. Simply enter the mass of reagent and the target concentration and the calculator will determine the rest.

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Preparation and Storage

Reconstitution
Reconstitute at 0.2 mg/mL in sterile PBS.
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Shipping
Lyophilized product is shipped at ambient temperature. Liquid small pack size (-SP) is shipped with polar packs. Upon receipt, store immediately at the temperature recommended below.
Stability & Storage
Use a manual defrost freezer and avoid repeated freeze-thaw cycles.
  • 12 months from date of receipt, -20 to -70 °C as supplied.
  • 1 month, 2 to 8 °C under sterile conditions after reconstitution.
  • 6 months, -20 to -70 °C under sterile conditions after reconstitution.

Background: Prolyl Oligopeptidase/PREP

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).

References
  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.
Entrez Gene IDs
5550 (Human); 19072 (Mouse); 83471 (Rat)
Alternate Names
dJ355L5.1 (prolyl endopeptidase); EC 3.4.21.26; MGC16060; PE; PEP; Post-proline cleaving enzyme; PREP; prolyl endopeptidase; Prolyl Oligopeptidase; rPop

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Citations for Human Prolyl Oligopeptidase/PREP Antibody

R&D Systems personnel manually curate a database that contains references using R&D Systems products. The data collected includes not only links to publications in PubMed, but also provides information about sample types, species, and experimental conditions.

3 Citations: Showing 1 - 3
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  1. Prolyl oligopeptidase enhances alpha-synuclein dimerization via direct protein-protein interaction.
    Authors: Savolainen M, Yan X, Myohanen T, Huttunen H
    J Biol Chem, 2015-01-02;290(8):5117-26.
    Species: Mouse
    Sample Types: Cell Lysates
    Applications: Western Blot
  2. The prolyl peptidases PRCP/PREP regulate IRS-1 stability critical for rapamycin-induced feedback activation of PI3K and AKT.
    Authors: Duan L, Ying G, Danzer B, Perez R, Shariat-Madar Z, Levenson V, Maki C
    J Biol Chem, 2014-06-16;289(31):21694-705.
    Species: Human
    Sample Types: Cell Lysates
    Applications: Western Blot
  3. Suppression of Tumor Growth in Mice by Rationally Designed Pseudopeptide Inhibitors of Fibroblast Activation Protein and Prolyl Oligopeptidase1
    Authors: Kenneth W. Jackson, Victoria J. Christiansen, Vivek R. Yadav, Robert Silasi-Mansat, Florea Lupu, Vibhudutta Awasthi et al.
    Neoplasia

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