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AB80376

Recombinant human Prolyl Endopeptidase protein

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(2 Publications)

Recombinant human Prolyl Endopeptidase protein is a Human Full Length protein, in the 2 to 710 aa range, expressed in Escherichia coli, with >90%, suitable for SDS-PAGE, FuncS.

View Alternative Names

PEP, PREP, Prolyl endopeptidase, PE, Post-proline cleaving enzyme

2 Images
Functional Studies - Recombinant human Prolyl Endopeptidase protein (AB80376)
  • FuncS

Unknown

Functional Studies - Recombinant human Prolyl Endopeptidase protein (AB80376)
SDS-PAGE - Recombinant human Prolyl Endopeptidase protein (AB80376)
  • SDS-PAGE

Unknown

SDS-PAGE - Recombinant human Prolyl Endopeptidase protein (AB80376)

Lane 1 : ab80376 on 10% SDS-PAGE, Coomassie staining, 4μg.
Lane 2 : Protein marker.

Key facts

Purity

>90% SDS-PAGE

Expression system

Escherichia coli

Tags

Tag free

Applications

FuncS, SDS-PAGE

applications

Biologically active

Yes

Biological activity

Specific Activity: ≥ 12 pmol/min/μg. Assay condition: 50 mM Tris (pH 7.5), 100 μg BSA, 20 μM substrate and 500 ng Prolyl Endopeptidase protein at room temperature for 30 min.

Accession

P48147

Animal free

No

Carrier free

No

Species

Human

Storage buffer

pH: 8 Constituents: 30% Glycerol (glycerin, glycerine), 0.58% Sodium chloride, 0.395% Tris HCl, 0.05% Sorbitan monolaurate, ethoxylated, 0.0462% (R*,R*)-1,4-Dimercaptobutan-2,3-diol

storage-buffer

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Reactivity data

{ "title": "Reactivity Data", "filters": { "stats": ["", "Reactivity", "Dilution Info", "Notes"] }, "values": { "SDS-PAGE": { "reactivity":"TESTED_AND_REACTS", "dilution-info":"", "notes":"<p></p>" }, "FuncS": { "reactivity":"TESTED_AND_REACTS", "dilution-info":"", "notes":"<p></p>" } } }
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Sequence info

[{"sequence":"MHHHHHHLSLQYPDVYRDETAVQDYHGHKICDPYAWLEDPDSEQTKAFVEAQNKITVPFLEQCPIRGLYKERMTELYDYPKYSCHFKKGKRYFYFYNTGLQNQRVLYVQDSLEGEARVFLDPNILSDDGTVALRGYAFSEDGEYFAYGLSASGSDWVTIKFMKVDGAKELPDVLERVKFSCMAWTHDGKGMFYNSYPQQDGKSDGTETSTNLHQKLYYHVLGTDQSEDILCAEFPDEPKWMGGAELSDDGRYVLLSIREGCDPVNRLWYCDLQQESSGIAGILKWVKLIDNFEGEYDYVTNEGTVFTFKTNRQSPNYRVINIDFRDPEESKWKVLVPEHEKDVLEWIACVRSNFLVLCYLHDVKNILQLHDLTTGALLKTFPLDVGSIVGYSGQKKDTEIFYQFTSFLSPGIIYHCDLTKEELEPRVFREVTVKGIDASDYQTVQIFYPSKDGTKIPMFIVHKKGIKLDGSHPAFLYGYGGFNISITPNYSVSRLIFVRHMGGILAVANIRGGGEYGETWHKGGILANKQNCFDDFQCAAEYLIKEGYTSPKRLTINGGSNGGLLVAACANQRPDLFGCVIAQVGVMDMLKFHKYTIGHAWTTDYGCSDSKQHFEWLVKYSPLHNVKLPEADDIQYPSMLLLTADHDDRVVPLHSLKFIATLQYIVGRSRKQSNPLLIHVDTKAGHGAGKPTAKVIEEVSDMFAFIARCLNVDWIP","proteinLength":"Full Length","predictedMolecularWeight":"81.6 kDa","actualMolecularWeight":null,"aminoAcidEnd":710,"aminoAcidStart":2,"nature":"Recombinant","expressionSystem":"Escherichia coli","accessionNumber":"P48147","tags":[]}]
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Properties and storage information

Shipped at conditions
Dry Ice
Appropriate short-term storage conditions
-80°C
Appropriate long-term storage conditions
-80°C
Aliquoting information
Upon delivery aliquot
Storage information
Avoid freeze / thaw cycle
True
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Supplementary information

This supplementary information is collated from multiple sources and compiled automatically.

Prolyl endopeptidase also known as prolyl oligopeptidase is a serine peptidase with a molecular mass of about 80 kDa. It specifically cleaves peptide bonds at the C-terminal side of proline residues within short peptides. Prolyl endopeptidase is expressed widely including in brain and peripheral tissues making it a significant target in various cellular processes. This enzyme features a catalytic triad typical of serine proteases which consists of serine histidine and aspartate residues.
Biological function summary

Prolyl endopeptidase participates in the modulation and degradation of proline-containing peptides impacting neuropeptide activity and peptide hormone regulation. It operates largely outside of any complex functioning independently in its enzymatic roles. Its activity influences processes such as cell signaling and neurotransmission by altering the lifespans of bioactive peptides contributing to cellular homeostasis and communication efficacy.

Pathways

Four enzymes interact in a cascade that includes prolyl endopeptidase within the renin-angiotensin system and other neuropeptide pathways. Particularly noteworthy is its involvement in the hydrolysis of small bioactive peptides which links it to proteins like angiotensin-converting enzyme. Prolyl endopeptidase manipulates peptide availability influencing blood pressure control and cognitive functions by its participation in peptide-related pathways.

Four enzymes are implicated in cognitive disorders and cardiovascular diseases with prolyl endopeptidase playing a considerable role. Its aberrant activity relates to neurodegenerative diseases such as Alzheimer's disease and conditions like hypertension. In Alzheimer's altered activity affects amyloid-beta peptide processing and interaction with tau protein while in hypertension its regulation or dysregulation impacts peptide substrates affiliated with blood pressure modulation.
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Specifications

Form

Liquid

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General info

Function

Cleaves peptide bonds on the C-terminal side of prolyl residues within peptides that are up to approximately 30 amino acids long.

Sequence similarities

Belongs to the peptidase S9A family.

Post-translational modifications

The N-terminus is blocked.

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Product protocols

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Target data

Cleaves peptide bonds on the C-terminal side of prolyl residues within peptides that are up to approximately 30 amino acids long.
See full target information PREP
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Publications (2)

Recent publications for all applications. Explore the full list and refine your search

Israel journal of chemistry 63: PubMed37982048

2023

DPP8/9 are not Required to Cleave Most Proline-Containing Peptides.

Applications

Unspecified application

Species

Unspecified reactive species

Abir Bhattacharjee,Daniel A Bachovchin

Molecular cell 73:446-457.e6 PubMed30612880

2019

Multisite Phosphorylation of S6K1 Directs a Kinase Phospho-code that Determines Substrate Selection.

Applications

Unspecified application

Species

Unspecified reactive species

Abul Arif,Jie Jia,Belinda Willard,Xiaoxia Li,Paul L Fox
View all publications
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