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PEPD encodes a member of the peptidase family. Additionally we are shipping Peptidase D Antibodies (51) and Peptidase D Kits (21) and many more products for this protein.
Showing 9 out of 11 products:
Increased serum prolidase activity and decreased antioxidant levels are likely to be a results of increased of oxidative stress levels in obese subjects
Serum prolidase activity is reduced in scleroderma patients, especially in diffuse form.
Increased levels of serum prolidase activity are associated with the severity of developmental dysplasia of the hip.
High resolution X-ray crystallographic models of substrate and product binding in the active site of human prolidase.
We report here that by introducing either the A252R or P365R substitution mutation, the structural changes affecting catalytic turnover rate and substrate binding affinity are valuable in improving the catalytic activity of human prolidase towards toxic organophosphorus compound hydrolysis.
In ankylosing spondylitis, serum prolidase level was successful in measuring disease activity
there is an independent relationship of aortic prolidase activity and aortic prolidase immunostaining with aortic stiffness beta index in patients who underwent coronary artery bypass grafting
Prolidase activity decreases in patients with chronic obstructive pulmonary disease.
absence of prolidase activity in pterygium tissue indicates that there is no collagen turnover in this tissue
Decreased serum prolidase activity may be associated with knee osteoarthritis
The findings identify peptidase D, an ubiquitously expressed intracellular peptidase, as a potential novel marker of colitis.
PEPD is a ligand of EGFR (show EGFR Proteins) and presents a novel mechanism of EGFR (show EGFR Proteins) activation
The dark-like mutation causes cardiomyocyte hypertrophy due to loss-of-function of peptidase d (Pepd).
NO stimulates prolidase activity by increasing serine/threonine phosphorylation through PKG (show PRKG1 Proteins)-cGMP pathway
This gene encodes a member of the peptidase family. The protein forms a homodimer that hydrolyzes dipeptides or tripeptides with C-terminal proline or hydroxyproline residues. The enzyme serves an important role in the recycling of proline, and may be rate limiting for the production of collagen. Mutations in this gene result in prolidase deficiency, which is characterized by the excretion of large amount of di- and tri-peptides containing proline. Multiple transcript variants encoding different isoforms have been found for this gene.
, X-Pro dipeptidase
, aminoacyl-L-proline hydrolase
, proline dipeptidase
, xaa-Pro dipeptidase
, X-pro dipeptidase
, peptidase 4