Prolyl Endopeptidase Proteins, Antibodies, cDNA Clones Research Reagents

All Prolyl Endopeptidase reagents are produced in house and quality controlled, including 1 Prolyl Endopeptidase Antibody, 32 Prolyl Endopeptidase Gene, 1 Prolyl Endopeptidase IP Kit, 1 Prolyl Endopeptidase Lysate, 1 Prolyl Endopeptidase Protein, 2 Prolyl Endopeptidase qPCR. All Prolyl Endopeptidase reagents are ready to use.

Prolyl Endopeptidase Protein (1)

    Prolyl Endopeptidase Antibody (1)

      Prolyl Endopeptidase cDNA Clone (32)


      In cloning vector

      In lentiviral vector

      Prolyl Endopeptidase Lysate (1)

        Prolyl Endopeptidase Background

        Prolyl endopeptidase, also known as PREP, belongs to a distinct class of serine peptidases. It is a large cytosolic enzyme which was first described in the cytosol of rabbit brain as an oligopeptidase. Prolyl endopeptidase degrades the nonapeptide bradykinin at the Pro-Phe bond. It is involved in the maturation and degradation of peptide hormones and neuropeptides such as alpha-melanocyte-stimulating hormone, luteinizing hormone-releasing hormone (LH-RH), thyrotropin-releasing hormone, angiotensin, neurotensin, oxytocin, substance P and vasopressin. Prolyl endopeptidase's activity is confined to action on oligopeptides of less than 1 kD and it has an absolute requirement for the trans-configuration of the peptide bond preceding proline. It cleaves peptide bonds at the C-terminal side of proline residues.

        Prolyl Endopeptidase References

        • Oliveira EB, et al. (1976) Isolation of brain endopeptidases: Influence of size and sequence of substrates structurally related to bradykinin. Biochemistry. 15(9):1967-74.
        • Stepniak D, et al. (2006) Highly efficient gluten degradation with a newly identified prolyl endoprotease: implications for celiac disease. Am J Physiol Gastrointest Liver Physiol. 291(4): G621-9.
        • Jarho EM, et al. (2007) 2(S)-(Cycloalk-1-enecarbonyl)-1-(4-phenyl-butanoyl)pyrrolidines and 2(S)-(aroyl)-1-(4-phenylbutanoyl)pyrrolidines as prolyl oligopeptidase inhibitors. Bioorg Med Chem. 15(5):2024-31.

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