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anti-Human CMA1 Anticorps:
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Human Monoclonal CMA1 Primary Antibody pour IHC (p), IHC - ABIN152116
Hsieh, Sharma, Gibbons, Goggans, Erzurum, Haque: Human airway epithelial cell determinants of survival and functional phenotype for primary human mast cells. dans Proceedings of the National Academy of Sciences of the United States of America 2005
Data show that chymase cleavage of chemerin (chem163S) to partially active chemerin (chem156F) can be found in synovial fluids where it can play a role in modulation of the inflammation in joints.
These findings reveal the critical role of hypoxia in producing local angiotensin II by a lactate-chymase-dependent mechanism and highlight the importance of local angiotensin II in regulating radioresistance of hypoxic tumor cells.
expression markedly increased in the maternal vascular endothelium in subjects with preeclampsia compared with normal pregnant controls
Cleavage of the alarmins by Human mast cell chymase and human neutrophil cathepsin G suggests a function in regulating excessive inflammation.
activation of endothelial CLP/chymase may directly relate to the increased inflammatory phenotypic changes in the vascular system in women with preeclampsia
Placenta-derived chymotrypsin-like protease contributes to the altered endothelial barrier function in preeclampsia.
promoter single nucleotide polymorphism is not associated with Dengue Hemorrhagic Fever and Dengue Shock Syndrome in Vietnam and Philippines
Our data demonstrated that mast cell chymase plays an important role in keloid formation through TGF-beta1/Smad signaling pathway.
These data suggest a possible contribution of human chymase activation to LPS-induced mortality
we present data indicating that MC tryptase and chymase contribute to the development of OSF and malignant transformation of the overlying epithelium.
The polymorphisms and haplotypes of the CMA1 locus are associated with cardiac hypertrophy in male patients with symptomatic aortic stenosis.
CMA1 gene single nucleotide polymorphisms is associated with essential hypertension.
Significant association between the AG genotype of CMA1 A polymorphism and Angina Pectoris and Ventricular Extrasystoles was observed.
The accumulated data in this review suggest that mast cells, their tryptases, and their chymases play important roles in tissue repair.
demonstrate the generation of Pso p27 from SCCA1 with extracts from psoriatic scale and even more remarkably, the generation of Pso p27 from SCCA1 in the presence of mast cell associated chymase
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.
Purified chymase mixed with fragmented heparin derived from heparanase-expressing cells show greater release from collagen gels than the enzyme alone or mixed with macromolecular heparin derived from mock cells.
Mast cell chymase degrades the alarmins heat shock protein 70, biglycan, HMGB1, and interleukin-33 (IL-33) and limits danger-induced inflammation.
Data indicate that the best Fynomer (the binding proteins derived from the Fyn SH3 domain) was found to bind chymase with a KD of 0.9 nM and koff of 6.6x10 (-4) s (-1) , and to selectively inhibit chymase activity with an IC 50 value of 2 nM.
Both IgE and chymase associate with diabetes status.
Mast cells have the ability to produce and degrade FXIIIA depending on their chymase expression profile: mast cells expressing chymase degrade FXIIIA, whereas mast cells that do not express chymase mainly produce FXIIIA
Fibronectin was identified as a target of mMCP-5, and the exocytosis of mMCP-5 from the MCs in the mouse's peritoneal cavity resulted in the expression of metalloproteinase protease-9, which has been implicated in arthritis.
Results suggest that mouse mast cell proteases 4, 5, and 6 are mediators of the critical role mast cells play in microdeformational wound therapy in the proliferative phase of healing.
Data indicate that a second-degree burn injury can initiate an immediate novel zonal degranulation of mast cell throughout all skin layers and a disruption of the epidermal tight junctions dependent on the nonredundant presence of mMCP4 and mMCP5.
mast cell/chymase-mediated intestinal epithelial barrier function is mediated by proteinase-activated receptor 2/MMP-2-dependent
mMCP-4-deficient mice but not to mMCP-5-deficient mice revealing nonredundant actions for these two MC proteases in a model of innate inflammatory injury with remodeling.
mast cell mMCP-4, -5, and -6 (chymase and tryptase) participate in the acute inflammation and remodeling process of viral myocarditis.
The prominent mast cell secretory granule protease MCP-5 is essential for the occurrence of irreversible ischemia-reperfusion injury of skeletal muscle.
mast cell chymase activates ERK and p38 probably through G-protein-coupled receptor, and the ERK but not p38 cascade may have a crucial role in chymase-induced migration of eosinophils
chymase rapidly cleaves recombinant pro-IL-18 at 56-phenylalanine and produces a biologically active IL-18 fragment that is smaller than any other reported IL-18-derived species
Cymase might play an important role in intermittent hypoxia-induced left ventricular remodeling, which is independent of the systemic blood pressure.
Just after stopping the angiotensin II infusion, aortic ACE and chymase activities were significantly increased, and were involved in the progression of aortic abdominal aneurysms
experimental abdominal aortic aneurysm in wild-type mice or those deficient in the chymase ortholog mouse mMCP-4 or deficient in mMCP-5 (Mcpt4(-/-), Mcpt5(-/-)), Mcpt4(-/-) but not Mcpt5(-/-) had reduced abdominal aortic aneurysm formation
This gene product is a chymotryptic serine proteinase that belongs to the peptidase family S1. It is expressed in mast cells and thought to function in the degradation of the extracellular matrix, the regulation of submucosal gland secretion, and the generation of vasoactive peptides. In the heart and blood vessels, this protein, rather than angiotensin converting enzyme, is largely responsible for converting angiotensin I to the vasoactive peptide angiotensin II. Angiotensin II has been implicated in blood pressure control and in the pathogenesis of hypertension, cardiac hypertrophy, and heart failure. Thus, this gene product is a target for cardiovascular disease therapies. This gene maps to 14q11.2 in a cluster of genes encoding other proteases.
, chymase 1 preproprotein transcript E
, chymase 1 preproprotein transcript I
, chymase, heart
, chymase, mast cell
, mast cell protease I
, mast cell chymase
, serine protease
, mast cell protease 2
, mast cell chymase 1
, mast cell protease 5
, mast cell protease 3
, mast cell protease III
, chymase 1, mast cell
, LOW QUALITY PROTEIN: chymase
, chymase like protein