Recombinant Human Prolyl Endopeptidase Protein

Name: Recombinant Human Prolyl Endopeptidase Protein
Brand: Beta LifeScience
SKU: BLA-7320P
Availability: InStock

Collections: Other recombinant proteins, Recombinant proteins

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Product Overview

Host Species	Human
Accession	P48147
Synonym	dJ355L5.1 (prolyl endopeptidase) HGNC:9358 MGC16060 OTTHUMP00000040498 PE PEP Post proline cleaving enzyme Post-proline cleaving enzyme PPCE_HUMAN Prep Prolyl endopeptidase Prolyl oligopeptidase
Description	Recombinant Human Prolyl Endopeptidase Protein was expressed in E.coli. It is a Full length protein
Source	E.coli
AA 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
Molecular Weight	83 kDa including tags
Purity	Greater than 90% SDS-PAGE
Endotoxin	< 1.0 EU per μg of the protein as determined by the LAL method
Formulation	Liquid Solution
Stability	The recombinant protein samples are stable for up to 12 months at -80°C
Reconstitution	See related COA
Unit Definition	For Research Use Only
Storage Buffer	Shipped at 4°C. Store at +4°C short term (1-2 weeks). Upon delivery aliquot. Store at -20°C or -80°C. Avoid freeze / thaw cycle.

Target Details

Target Function	Cleaves peptide bonds on the C-terminal side of prolyl residues within peptides that are up to approximately 30 amino acids long.
Subcellular Location	Cytoplasm.
Protein Families	Peptidase S9A family
Database References	HGNC: 9358 OMIM: 600400 KEGG: hsa:5550 STRING: 9606.ENSP00000358106 UniGene: Hs.436564

Gene Functions References

These findings provide evidence for newly-discovered roles for PREP in mechanisms regulating cellular plasticity through NCAM and PSA-NCAM. PMID: 27566163
Study shows that the expression of POP increases with hepatocyte steatosis suggesting an important role in hepatocytes steatosis and possibly NAFLD. PMID: 27760195
It was found that human PREP behaves identically to the porcine homolog, displaying a double bell-shaped pH profile and a pH-dependent solvent kinetic isotope effect of the kcat/Km, features that set it apart from the related exopeptidase dipeptidyl peptidase IV (DPP IV). PMID: 28062644
TLR4 activation releases prolyl endopeptidase containing exosomes from airway epithelial cells. PMID: 26222144
This study found that circulating PREP activity was substantially reduced in all cirrhotic patients but those changes did not have evident correlation to hepatic encephalopathy. PMID: 26420028
PEP was significantly and positively associated with delinquent, aggressive, externalizing and internalizing behavior subscales. PMID: 26165750
PREP redox inactivation is due to oxidation of cysteine residues and consequent oligomerization through intermolecular disulfide bonds. PMID: 25236746
Data indicate that SAXS analysis showed that presequence protease (hPreP) open states and substrate binding dynamics. PMID: 24931469
The determination of PEP activity in the plasma may be a safe, minimally invasive and inexpensive way to define the aggressiveness of CRC in daily practice. PMID: 24465166
first demonstration of colocalization of PREP and pathological proteins in the human brain, supporting the view that, at least in spatial terms, PREP could be associated with pathogenesis of neurodegenerative diseases PMID: 23562579
These results indicate that POP may be a positive regulator of cell cycle progression by regulating the exit from and/or reentry into the cell cycle by KATO III cells. PMID: 24269815
interaction between prolyl oligopeptidase and glyceraldehyde-3-phosphate dehydrogenase is required for cytosine arabinoside-induced glyceraldehyde-3-phosphate dehydrogenase nuclear translocation and cell death PMID: 23348613
Oxidative stress and the levels of endogenous plasma prolyl oligopeptidase (PREP) inhibitor alpha-2-macroglobulin (alpha2M) decrease PREP activity in multiple sclerosis patients. PMID: 23643808
PREP may be associated with secretory processes as well as in reproduction. A more abundant expression of PREP in malignant than benign tumors suggests that PREP may be associated with expansion and metastasis of tumors. PMID: 22740343
analysis of the substrate preferences of two post-proline cleaving endopeptidases, prolyl oligopeptidase and fibroblast activation protein alpha PMID: 22750443
PREP is a regulatory target and a regulatory element in cell signalling. This is the first report of a direct influence of a cell signalling molecule, retinoic acid, on PREP expression. PMID: 21487212
Molecular modeling and docking based approaches were used to unravel questions like differences in ligand binding affinities in three POP species (porcine, human and A. thaliana). PMID: 22132071
These results indicate that POP is a part of the machinery that controls the cell cycle. PMID: 21620802
Results indicate that there is no strong and direct interaction between POP and GAP43 at physiological conditions. PMID: 20869470
The constitutive expression of PREP mRNA in chronic lymphocytic leukemia was demonstrated. PMID: 20534982
Cytosolic Prolyl endopeptidase activity significantly increased in clear cell renal cell carcinoma, urothelial carcinoma of the renal pelvis and head and neck squamous cell carcinoma. PMID: 20362629
Plasma levels of PREP activity as well as those of their endogenous inhibitor are suggested as biomarkers of inflammation and oxidative stress in multiple sclerosis PMID: 20370893
The high activity of prolyl endopeptidase in the human cortex suggests that prolyl endopeptidase could play a role in cortical functions. Activity in humans is highest in the frontal lobe and cytosolic fractions. PMID: 11792464
The activities of pyroglutamyl peptidase I and prolyl endopeptidase in necrozoospermia were found to be higher in the corresponding soluble and particulate sperm fractions, respectively, with respect to those measured in normozoospermic semen PMID: 15380924
primary structure, recombinant expression and homology modelling of brain prolyl oligopeptidase PMID: 15838896
Mainly localized to perinuclear space and associated with microtubulin cytoskeleton in human neuroblastoma and glioma. Novel functions in axonal transport and/or protein secretion. PEP inhibitors may be useful in variety of related clinical conditions. PMID: 16092940
data demonstrate for the first time prolyl endopeptidase turnover of humanin by a limited post-cysteine as well as post-proline proteolysis resulting in the inactivation of this potentially apoptosis-related factor PMID: 16700513
Results describe the distribution of immunoreactive prolyl oligopeptidase in human and rat brain. PMID: 17401647
The results rule out a causative role of POP in the pathogenesis of CD and strongly suggest that other peptidases are needed to eliminate gliadin-derived, immunoactive and toxic peptides larger than 33-mer, which is a POP inhibitor. PMID: 17454876
Data reveal for the first time the presence of a new side opening in prolyl oligopeptidase that was not observed in any of the crystallographic structures described to date. PMID: 19782684

FAQs

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Proteins are sensitive to heat, and freeze-drying can preserve the activity of the majority of proteins. It improves protein stability, extends storage time, and reduces shipping costs. However, freeze-drying can also lead to the loss of the active portion of the protein and cause aggregation and denaturation issues. Nonetheless, these adverse effects can be minimized by incorporating protective agents such as stabilizers, additives, and excipients, and by carefully controlling various lyophilization conditions.

Commonly used protectant include saccharides, polyols, polymers, surfactants, some proteins and amino acids etc. We usually add 8% (mass ratio by volume) of trehalose and mannitol as lyoprotectant. Trehalose can significantly prevent the alter of the protein secondary structure, the extension and aggregation of proteins during freeze-drying process; mannitol is also a universal applied protectant and fillers, which can reduce the aggregation of certain proteins after lyophilization.

Our protein products do not contain carrier protein or other additives (such as bovine serum albumin (BSA), human serum albumin (HSA) and sucrose, etc., and when lyophilized with the solution with the lowest salt content, they often cannot form A white grid structure, but a small amount of protein is deposited in the tube during the freeze-drying process, forming a thin or invisible transparent protein layer.

Reminder: Before opening the tube cap, we recommend that you quickly centrifuge for 20-30 seconds in a small centrifuge, so that the protein attached to the tube cap or the tube wall can be aggregated at the bottom of the tube. Our quality control procedures ensure that each tube contains the correct amount of protein, and although sometimes you can't see the protein powder, the amount of protein in the tube is still very precise.

To learn more about how to properly dissolve the lyophilized recombinant protein, please visit Lyophilization FAQs.