Abcam, ab80376, Recombinant human Prolyl Endopeptidase protein

Size: 20µg
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.
Key facts
Purity:>90% SDS-PAGE,
Expression system:Escherichia coli,
Tags:Tag free,
Applications:FuncS, SDS-PAGESee reactivity dataSee the reactivity data table below for information on validated species and application combinations.,
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: 8Constituents: 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

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

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.