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The protein encoded by PREP is a cytosolic prolyl endopeptidase that cleaves peptide bonds on the C-terminal side of prolyl residues within peptides that are up to approximately 30 amino acids long. Additionally we are shipping Prolyl Endopeptidase Antibodies (67) and Prolyl Endopeptidase Kits (9) and many more products for this protein.
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These findings provide evidence for newly-discovered roles for PREP in mechanisms regulating cellular plasticity through NCAM (show NCAM1 Proteins) and PSA (show PLAG1 Proteins)-NCAM (show NCAM1 Proteins).
Study shows that the expression of POP increases with hepatocyte steatosis suggesting an important role in hepatocytes steatosis and possibly NAFLD.
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 (show DPP4 Proteins)).
TLR4 (show TLR4 Proteins) activation releases prolyl endopeptidase containing exosomes from airway epithelial cells.
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.
PEP was significantly and positively associated with delinquent, aggressive, externalizing and internalizing behavior subscales.
PREP redox inactivation is due to oxidation of cysteine residues and consequent oligomerization through intermolecular disulfide bonds.
Data indicate that SAXS analysis showed that presequence protease (hPreP (show PITRM1 Proteins)) open states and substrate binding dynamics.
The determination of PEP (show PAEP Proteins) activity in the plasma may be a safe, minimally invasive and inexpensive way to define the aggressiveness of CRC (show CALR Proteins) in daily practice.
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
Ion mobility mass spectrometry (IMMS) experiments detected two species of PREP that correlated well with the open and closed conformations in dynamic equilibrium. Therefore, these findings emphasize the value of IMMS for the study of multiple co-existing conformations of large proteins in slow equilibrium in solution.
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).
These findings might be explained as possible alteration in brain plasticity caused by PREP deficiency, which in turn affect behaviour and brain development
Lung ischemia-reperfusion injury causes a dysregulation of circulating Ang 2 (show ANGPT2 Proteins) levels and plasma PREP activity, although no direct link between both phenomena could be shown.
the expression of prolyl endopeptidase could be necessary for a correct reproductive function
As PREP inhibition also enhances autophagic clearance of aSyn, PREP inhibitors may reduce accumulation of aSyn inclusions via a dual mechanism and are thus a novel therapeutic candidate for synucleinopathies.
lncPrep+96kb could play a role in the POP gene activation in the granulosa cell.
PREP knockdown mice (Prep(gt/gt (show FABP6 Proteins))) exhibited glucose intolerance, decreased fasting insulin (show INS Proteins), increased fasting glucagon (show GCG Proteins) levels, and reduced glucose-induced insulin (show INS Proteins) secretion compared with wild-type controls.
The study reveals a role for prolyl endopeptidase in mediating hippocampal plasticity and spatial memory formation.
The POP promoter was sufficient for the appropriate localization in the placenta if it was not subject to position effect.
the cytoplasmic and membrane-associated POP have distinct roles in different types of placental cells.
The protein encoded by this gene is a cytosolic prolyl endopeptidase that cleaves peptide bonds on the C-terminal side of prolyl residues within peptides that are up to approximately 30 amino acids long. Prolyl endopeptidases have been reported to be involved in the maturation and degradation of peptide hormones and neuropeptides.
, Prolyl endopeptidase
, dJ355L5.1 (prolyl endopeptidase)
, post-proline cleaving enzyme
, prolyl oligopeptidase