O9515
Prolyl oligopeptidase
recombinant, expressed in E. coli
Synonyme(s) :
Prolyl endopeptidase
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About This Item
Code UNSPSC :
12352204
Nomenclature NACRES :
NA.54
Produits recommandés
Produit recombinant
expressed in E. coli
Niveau de qualité
Pureté
≥90% (SDS-PAGE)
Forme
solution
Activité spécifique
≥10 unit/μg protein
Poids mol.
81.6 kDa
Conditions d'expédition
dry ice
Température de stockage
−70°C
Description générale
Prolyl oligopeptidase (PO) is mapped to human chromosome 6q22. It comprises of a N-terminal β-propeller domain and C-terminal α/β hydrolase catalytic domain. PO is highly expressed in the neuronal cytoplasm and its expression increases with age.
Prolyl oligopeptidase is a cytosolic serine peptidase which cleaves peptide bonds at the C′ terminal side of prolines. It is only capable of processing peptides containing no more than 30 amino acids due to the unique β-propeller region that regulates access to the active site.
Application
Prolyl oligopeptidase has been used in a study to assess the mechanism of lithium ion action. It has also been used in a study to investigate its distribution in human tissue and body fluids.
Prolyl oligopeptidase has been used in the prolyl oligopeptidase inhibitory activity assay in lyophilized protein hydrolysate samples and Schistosoma mansoni samples.
Actions biochimiques/physiologiques
Prolyl oligopeptidase (PO) regulates physiological processes and is crucial for the generation of active hormone and peptide fragments from their precursors. It shows elevated levels in psychiatric disorders and Alzheimer′s patients. Altered levels of PO is observed in patients with bipolar disorder. High expression of PO may promote metastasis of malignant ovarian and colorectal tumors.
Définition de l'unité
One unit will hydrolyze 1.0 picomole of Ala-Pro-aminomethylcoumarin per minute at pH 7.4 at 25 °C.
Forme physique
Supplied as a solution in 45 mM Tris-HCl, pH 8.0, 124 mM NaCl, 2.4 mM KCl, 10% glycerol, 3 mM DTT and variable amounts of imidazole.
Notes préparatoires
N-terminal GST-tagged 81.6 kDa full-length protein
Code de la classe de stockage
12 - Non Combustible Liquids
Classe de danger pour l'eau (WGK)
WGK 1
Point d'éclair (°F)
Not applicable
Point d'éclair (°C)
Not applicable
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Les clients ont également consulté
R S Williams et al.
The EMBO journal, 18(10), 2734-2745 (1999-05-18)
The therapeutic properties of lithium ions (Li+) are well known; however, the mechanism of their action remains unclear. To investigate this problem, we have isolated Li+-resistant mutants from Dictyostelium. Here, we describe the analysis of one of these mutants. This
Structure-function properties of prolyl oligopeptidase family enzymes
Rea D and Fulop V
Cell Biochemistry and Biophysics, 44(3), 349-365 (2006)
Mechanism of Action of Prolyl Oligopeptidase (PREP) in Degenerative Brain Diseases: Has Peptidase Activity Only a Modulatory Role on the Interactions of PREP with Proteins?
Mannisto PT, et al.
Frontiers in Aging Neuroscience, 9(3), 27-27 (2017)
Distribution of Prolyl Oligopeptidase in Human Peripheral Tissues and Body Fluids
Goossens, F., et al.
Clinical Chemistry and Laboratory Medicine, 34, 17-22 null
Prolyl oligopeptidase from the blood fluke Schistosoma mansoni: from functional analysis to anti-schistosomal inhibitors
Fajtova P, et al.
PLoS Neglected Tropical Diseases, 9(6), e0003827-e0003827 (2015)
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