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The protein encoded by PRCP is a lysosomal prolylcarboxypeptidase, which cleaves C-terminal amino acids linked to proline in peptides such as angiotension II, III and des-Arg9-bradykinin. De plus, nous expédions Prolylcarboxypeptidase Kits (55) et Prolylcarboxypeptidase Protéines (11) et beaucoup plus de produits pour cette protéine.
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Prolylcarboxypeptidase (PRCP) converts AngII to Ang (1-7) but only at an acidic pH. Global PRCP deficiency causes heart and kidney alterations and a moderate rise in BP. PRCP is abundant in the kidney collecting tubules, where the prevailing pH is low. In collecting tubules, PRCP deficiency could result in impaired AngII degradation. Increased AngII at this nephron site stimulates Na reabsorption and increases BP.
activity and expression in plasma and lung tissue stays unaffected in lung ischemia-reperfusion injury
This study demonistrated that PRCP gene is broadly expressed in the brain.
PRCP regulates cell growth, angiogenesis, and the response to vascular injury
ACE2 metabolizes ANG II in the kidney at neutral and basic pH, while prolylcarboxypeptidase catalyzes the same reaction at acidic pH.
PRCP is an important regulator of energy and glucose homeostasis since its deletion significantly improves metabolic parameters in mice exposed to both standard chow diet and high-fat diet
analysis of non-benzimidazole and brain-penetrant prolylcarboxypeptidase inhibitors
This study showed that PRCP mutant mice have a significant decrease in fat mass, although an increase in lean mass was also observed; reduced leptin levels and increased energy expenditure were also found.
Murine prolylcarboxypeptidase depletion induces vascular dysfunction with hypertension and faster arterial thrombosis.
PRCP is an important component of melanocortin signaling and weight maintenance via control of active alpha-MSH1-13 levels.
For the first time, PRCP is identified as an apelin-cleaving enzyme.
The decrease in PRCP levels in the first 24 h after stroke onset is associated with stroke severity and an unfavourable short-term stroke outcome
PRCP1 interacts with plasma kallikrein (PK) at multiple sites for PK activation.
The present results indicated PRCP rs7104980 can be considered as a marker for EH and Hap3 GAGCACTAACA (PRCP) and Hap16 TTTA (CMA1) might be associated with essential hypertension in Chinese Han population.
PRCP as a resistance factor for 4OHTAM resistance in estrogen receptor-positive breast cancer cells.
A single peptide, with the sequence YPRPIHPA, as a novel substrate for PRCP in human cerebrospinal fluid.
Purified PrCP yielded crystals belonging to space group R32, with unit-cell parameters a = b = 181.14, c = 240.13 A, that diffracted to better than 2.8 A resolution.
A structure-based alignment with the previously undescribed structure of DPP7 illuminates the mechanism of orthogonal substrate specificity of PRCP and DPP7.
Data suggest that the E112D polymorphism in the PRCP gene may be a useful genetic marker to predict the antihypertensive effect of short-term benazepril treatment in hypertensive patients.
PRCP appears to be a HUVEC-associated prekallikrein activator.
Identification of prolylcarboxypeptidase as the cell matrix-associated prekallikrein activator.
recombinant protein, identical to enzyme from human umbilical vein endothelial cells, is a prekallikrein activator.
Prolylcarboxypepdiase E112D (rs2298668)D allele alone and jointly with chronic hypertension were associated with a significantly increased risk of preeclampsia
role in regulation cardiovascular tone; proinflammatory agent
These investigations showed that the C-terminal region of the rPRCP(40) contributes to PRCP's catalytic function, and provided additional experimental evidence for this suggestion.
The protein encoded by this gene is a lysosomal prolylcarboxypeptidase, which cleaves C-terminal amino acids linked to proline in peptides such as angiotension II, III and des-Arg9-bradykinin. The cleavage occurs at acidic pH, but the enzyme activity is retained with some substrates at neutral pH. This enzyme has been shown to be an activator of the cell matrix-associated prekallikrein. The importance of angiotension II, one of the substrates of this enzyme, in regulating blood pressure and electrolyte balance suggests that this gene may be related to essential hypertension. Alternatively spliced transcript variants encoding distinct isoforms have been observed.
, lysosomal Pro-X carboxypeptidase
, proline carboxypeptidase
, angiotensinase C
, lysosomal carboxypeptidase C
, prolylcarboxypeptidase isoform 1 preproprotein