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PEPD encodes a member of the peptidase family. Additionally we are shipping Peptidase D Antibodies (48) and Peptidase D Kits (12) and many more products for this protein.
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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 association between the PEPD genetic variant and the risk of T2D was modulated by n-3 fatty acids. Higher n-3 fatty acids may abolish the adverse effect of the risk allele at PEPD for T2D
Prolidase was required for IFNAR1 (show IFNAR1 Proteins) maturation and accumulation, activation of IFNbeta-stimulated gene induction, and IFN-I-dependent viral control.
Levels of both serum prolidase and AFP (show AFP Proteins) could contribute to the early diagnosing of hepatocellular carcinoma.
Serum prolidase level was significantly higher in schizophrenia patients compared to the controls.
There may be an ethnic- and/or sex-specific association of the PEPD rs731839 single nucleotide polymorphism and serum lipid levels in Mulao and Han populations
Prolidase is required for early trafficking events during influenza A virus entry.
High prolidase activity may indicate critical biological activities relevant to pathological events in Behcet's disease, and this activity may be a biological indicator of disease.
Significantly lower prolidase activity in patients with benign joint hypermobility syndrome suggests that prolidase may affect the collagen metabolism and cause hyperlaxity.
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