PREP Human

Prolyl Endopeptidase Human Recombinant
Cat. No.
BT24254
Source
Escherichia Coli.
Synonyms
Prolyl Endopeptidase, Post-Proline Cleaving Enzyme, EC 3.4.21.26, PEP, PE, DJ355L5.1 (Prolyl Endopeptidase), Prolyl Oligopeptidase, Prolyl endopeptidase.
Appearance
Sterile filtered colorless solution.
Purity
Greater than 90.0% as determined by SDS-PAGE.
Usage
THE BioTek's products are furnished for LABORATORY RESEARCH USE ONLY. They may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Description

PREP Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 733 amino acids (1-710 a.a) and having a molecular mass of 83.1kDa.
PREP is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Product Specs

Introduction
Prolyl Endopeptidase, also known as PREP, is a cytosolic enzyme that breaks down peptide bonds. It specifically targets peptide bonds located on the C-terminal side of proline amino acid residues within peptides that are approximately 30 amino acids long. PREP plays a crucial role in the maturation and degradation of peptide hormones and neuropeptides.
Description
Recombinant human PREP, expressed in E. coli, is a single polypeptide chain without any glycosylation modifications. It consists of 733 amino acids, with a truncated sequence spanning from amino acid positions 1 to 710, resulting in a molecular weight of 83.1 kDa. The recombinant PREP protein features a 23-amino acid Histidine tag (His-tag) at its N-terminus to facilitate purification, which is achieved through proprietary chromatographic methods.
Physical Appearance
Clear and colorless solution that has been sterilized by filtration.
Formulation
The PREP protein solution is provided at a concentration of 0.25 mg/ml and is prepared in a buffer consisting of phosphate-buffered saline (PBS) at pH 7.4, 30% glycerol, and 1mM dithiothreitol (DTT).
Stability
For short-term storage (2-4 weeks), the PREP protein solution should be kept at 4°C. For extended storage, it is recommended to freeze the solution at -20°C. Adding a carrier protein such as albumin (HSA or BSA) at a concentration of 0.1% is advisable for long-term storage. Repeated freezing and thawing of the protein solution should be avoided.
Purity
The purity of PREP is determined to be greater than 90% using SDS-PAGE analysis.
Synonyms
Prolyl Endopeptidase, Post-Proline Cleaving Enzyme, EC 3.4.21.26, PEP, PE, DJ355L5.1 (Prolyl Endopeptidase), Prolyl Oligopeptidase, Prolyl endopeptidase.
Source
Escherichia Coli.
Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSMLSLQYP DVYRDETAVQ DYHGHKICDP YAWLEDPDSE QTKAFVEAQN KITVPFLEQC PIRGLYKERM TELYDYPKYS CHFKKGKRYF YFYNTGLQNQ RVLYVQDSLE GEARVFLDPN ILSDDGTVAL RGYAFSEDGE YFAYGLSASG SDWVTIKFMK VDGAKELPDV LERVKFSCMA WTHDGKGMFY NSYPQQDGKS DGTETSTNLH QKLYYHVLGT DQSEDILCAE FPDEPKWMGG AELSDDGRYV LLSIREGCDP VNRLWYCDLQ QESSGIAGIL KWVKLIDNFE GEYDYVTNEG TVFTFKTNRQ SPNYRVINID FRDPEESKWK VLVPEHEKDV LEWIACVRSN FLVLCYLHDV KNILQLHDLT TGALLKTFPL DVGSIVGYSG QKKDTEIFYQ FTSFLSPGII YHCDLTKEEL EPRVFREVTV KGIDASDYQT VQIFYPSKDG TKIPMFIVHK KGIKLDGSHP AFLYGYGGFN ISITPNYSVS RLIFVRHMGG ILAVANIRGG GEYGETWHKG GILANKQNCF DDFQCAAEYL IKEGYTSPKR LTINGGSNGG LLVAACANQR PDLFGCVIAQ VGVMDMLKFH KYTIGHAWTT DYGCSDSKQH FEWLVKYSPL HNVKLPEADD IQYPSMLLLT ADHDDRVVPL HSLKFIATLQ YIVGRSRKQS NPLLIHVDTK AGHGAGKPTA KVIEEVSDMF AFIARCLNVD WIP.

Product Science Overview

Introduction

Prolyl Endopeptidase (PE), also known as Prolyl Oligopeptidase (POP) or PREP, is a cytosolic enzyme that belongs to the serine peptidase family. This enzyme is encoded by the PREP gene in humans and plays a crucial role in the maturation and degradation of peptide hormones and neuropeptides .

Structure and Function

Prolyl Endopeptidase is a large enzyme with a molecular mass of approximately 81 kDa . It cleaves peptide bonds at the C-terminal side of proline residues within peptides that are up to approximately 30 amino acids long . The enzyme’s activity is confined to oligopeptides of less than 10 kDa and requires the trans-configuration of the peptide bond preceding proline .

The enzyme’s structure includes a distinct beta-propeller region that acts as a gating filter mechanism, allowing only short protein residues to enter the active site . This specificity enables Prolyl Endopeptidase to hydrolyze a variety of biologically active peptides such as bradykinin, substance P, neurotensin, and vasopressin .

Biological Significance

Prolyl Endopeptidase is involved in several critical biological processes, including the maturation and degradation of peptide hormones and neuropeptides . Some of the key peptides hydrolyzed by this enzyme include:

  • Bradykinin: A peptide that causes blood vessels to dilate, leading to a drop in blood pressure.
  • Substance P: A neuropeptide involved in the transmission of pain and other sensory signals.
  • Neurotensin: A peptide that modulates dopamine signaling and has various effects on the central nervous system.
  • Vasopressin: A hormone that regulates water retention in the body .
Recombinant Production

Recombinant Human Prolyl Endopeptidase is produced using baculovirus expression systems in insect cells (Spodoptera frugiperda, Sf 21) . The recombinant enzyme is typically tagged with a 6-His tag for purification purposes and is supplied as a carrier-free formulation to avoid interference from other proteins .

Applications

Recombinant Prolyl Endopeptidase is widely used in biochemical research to study its role in peptide hormone regulation and neuropeptide degradation. It is also utilized in drug development to explore potential therapeutic targets for conditions related to peptide hormone imbalances and neurodegenerative diseases .

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