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AB58988

Anti-Prolyl Endopeptidase antibody

4

(1 Review)

|

(23 Publications)

Rabbit Polyclonal Prolyl Endopeptidase antibody. Suitable for WB and reacts with Dog samples. Cited in 23 publications. Immunogen corresponding to Synthetic Peptide within Human PREP.

View Alternative Names

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

1 Images
Western blot - Anti-Prolyl Endopeptidase antibody (AB58988)
  • WB

Unknown

Western blot - Anti-Prolyl Endopeptidase antibody (AB58988)

All lanes:

Western blot - Anti-Prolyl Endopeptidase antibody (ab58988) at 1/1000 dilution

Lane 1:

Madin Darby canine kidney (MDCK) cell lysate at 10 µL

Lane 2:

Madin Darby canine kidney (MDCK) cell lysate at 5 µL

Predicted band size: 81 kDa

false

Key facts

Host species

Rabbit

Clonality

Polyclonal

Isotype

IgG

Carrier free

No

Reacts with

Dog

Applications

WB

applications

Immunogen

Synthetic Peptide within Human PREP. The exact immunogen used to generate this antibody is proprietary information.

P48147

Specificity

ab58988 does not recognize other Prolyl Endopeptidase family members.

Reactivity data

{ "title": "Reactivity Data", "filters": { "stats": ["", "Species", "Dilution Info", "Notes"], "tabs": { "all-applications": {"fullname" : "All Applications", "shortname": "All Applications"}, "WB" : {"fullname" : "Western blot", "shortname":"WB"} }, "product-promise": { "all": "all", "testedAndGuaranteed": "tested", "guaranteed": "expected", "predicted": "predicted", "notRecommended": "not-recommended" } }, "values": { "Dog": { "WB-species-checked": "testedAndGuaranteed", "WB-species-dilution-info": "1/1000 - 1/5000", "WB-species-notes": "<p></p>" } } }

Properties and storage information

Form
Liquid
Purification technique
Affinity purification Immunogen
Storage buffer
pH: 7.4 Preservative: 0.05% Sodium azide Constituents: PBS, 50% Glycerol (glycerin, glycerine), 2.9% Sodium chloride
Shipped at conditions
Blue Ice
Appropriate short-term storage conditions
+4°C
Appropriate long-term storage conditions
-20°C
Storage information
Stable for 12 months at -20°C

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.

Product protocols

For this product, it's our understanding that no specific protocols are required. You can visit:

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

Publications (23)

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

Journal of medicinal chemistry 67:5421-5436 PubMed38546708

2024

5-Aminothiazoles Reveal a New Ligand-Binding Site on Prolyl Oligopeptidase Which is Important for Modulation of Its Protein-Protein Interaction-Derived Functions.

Applications

Unspecified application

Species

Unspecified reactive species

Henri T Pätsi,Tommi P Kilpeläinen,Mikael Jumppanen,Johanna Uhari-Väänänen,Pieter Van Wielendaele,Francesca De Lorenzo,Hengjing Cui,Samuli Auno,Janne Saharinen,Erin Seppälä,Nina Sipari,Juha Savinainen,Ingrid De Meester,Anne-Marie Lambeir,Maija Lahtela-Kakkonen,Timo T Myöhänen,Erik A A Wallén

Experimental & molecular medicine 55:1437-1450 PubMed37394591

2023

Prolyl endopeptidase remodels macrophage function as a novel transcriptional coregulator and inhibits fibrosis.

Applications

Unspecified application

Species

Unspecified reactive species

Shuang-Zhe Lin,Wei-Jie Wu,Yu-Qing Cheng,Jian-Bin Zhang,Dai-Xi Jiang,Tian-Yi Ren,Wen-Jin Ding,Mingxi Liu,Yuan-Wen Chen,Jian-Gao Fan

Journal of medicinal chemistry 66:7475-7496 PubMed37248563

2023

Nonpeptidic Oxazole-Based Prolyl Oligopeptidase Ligands with Disease-Modifying Effects on α-Synuclein Mouse Models of Parkinson's Disease.

Applications

Unspecified application

Species

Unspecified reactive species

Tommi P Kilpeläinen,Henri T Pätsi,Reinis Svarcbahs,Ulrika H Julku,Tony S Eteläinen,Hengjing Cui,Samuli Auno,Nina Sipari,Susanna Norrbacka,Teppo O Leino,Maria Jäntti,Timo T Myöhänen,Erik A A Wallén

Journal of clinical and translational hepatology 11:1035-1049 PubMed37577240

2023

Therapeutic Effect of Prolyl Endopeptidase Inhibitor in High-fat Diet-induced Metabolic Dysfunction-associated Fatty Liver Disease.

Applications

Unspecified application

Species

Unspecified reactive species

Jian-Bin Zhang,Meng-Ting Li,Shuang-Zhe Lin,Yu-Qing Cheng,Jian-Gao Fan,Yuan-Wen Chen

International journal of molecular sciences 23: PubMed35563519

2022

New Insight on the In Vitro Effects of Melatonin in Preserving Human Sperm Quality.

Applications

Unspecified application

Species

Unspecified reactive species

Sergio Minucci,Massimo Venditti

Biomedicine & pharmacotherapy = Biomedecine & pharmacotherapie 146:112501 PubMed34891119

2021

Inhibition of prolyl oligopeptidase: A promising pathway to prevent the progression of age-related macular degeneration.

Applications

Unspecified application

Species

Unspecified reactive species

Laura Hellinen,Ali Koskela,Elina Vattulainen,Mikko Liukkonen,Christine Wegler,Andrea Treyer,Niklas Handin,Richard Svensson,Timo Myöhänen,Antti Poso,Kai Kaarniranta,Per Artursson,Arto Urtti

International journal of molecular sciences 22: PubMed34360857

2021

Preliminary Investigation on the Involvement of Cytoskeleton-Related Proteins, DAAM1 and PREP, in Human Testicular Disorders.

Applications

Unspecified application

Species

Unspecified reactive species

Massimo Venditti,Davide Arcaniolo,Marco De Sio,Sergio Minucci

Life sciences 270:119131 PubMed33516698

2021

Prolyl endopeptidase disruption reduces hepatic inflammation and oxidative stress in methionine-choline-deficient diet-induced steatohepatitis.

Applications

Unspecified application

Species

Unspecified reactive species

Jianbin Zhang,Daixi Jiang,Shuangzhe Lin,Yuqing Cheng,Jiaxing Pan,Wenjin Ding,Yuanwen Chen,Jiangao Fan

Animals : an open access journal from MDPI 11: PubMed33435542

2021

Preliminary Investigation on the Ameliorative Role Exerted by D-Aspartic Acid in Counteracting Ethane Dimethane Sulfonate (EDS) Toxicity in the Rat Testis.

Applications

Unspecified application

Species

Unspecified reactive species

Massimo Venditti,Maria Zelinda Romano,Francesco Aniello,Sergio Minucci

Biomedicines 8: PubMed33322134

2020

The Inhibition of Prolyl Oligopeptidase as New Target to Counteract Chronic Venous Insufficiency: Findings in a Mouse Model.

Applications

Unspecified application

Species

Unspecified reactive species

Giovanna Casili,Marika Lanza,Sarah Adriana Scuderi,Salvatore Messina,Irene Paterniti,Michela Campolo,Emanuela Esposito
View all publications

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