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The protein encoded by CTSE is a gastric aspartyl protease that functions as a disulfide-linked homodimer. De plus, nous expédions Cathepsin E Protéines (22) et Cathepsin E Kits (15) et beaucoup plus de produits pour cette protéine.
Showing 10 out of 54 products:
Human Polyclonal Cathepsin E Primary Antibody pour EIA, WB - ABIN452887
Caruso, Moore, Goodall, Thomas, Phillis, Tyskin, Cheetham, Lerda, Takahashi, Ruszkiewicz: Over-expression of cathepsin E and trefoil factor 1 in sessile serrated adenomas of the colorectum identified by gene expression analysis. dans Virchows Archiv : an international journal of pathology 2009
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Mouse (Murine) Polyclonal Cathepsin E Primary Antibody pour ELISA - ABIN2001133
Azuma, Pals, Mohandas, Couvreur, Taggart: Human gastric cathepsin E. Predicted sequence, localization to chromosome 1, and sequence homology with other aspartic proteinases. dans The Journal of biological chemistry 1989
Cathepsin E, mitochondrial fission, and caspase (Montrer CASP3 Anticorps) activation/apoptosis are linked in the pathogenesis of pulmonary emphysema.
High Expression of Cathepsin E is associated with Tissues but Not Blood of Patients with Barrett's Esophagus and Adenocarcinoma.
Decreased activity of cathepsin E produced by decidual macrophages might be responsible for the induction of miscarriages in some recurrent miscarriage patients.
data demonstrate that CatE contributes to normal growth and development of mammary glands through proper trafficking and secretion of Wnt5a (Montrer WNT5A Anticorps)
CTSE is a marker of both gastric differentiation and signet-ring cell carcinoma, which should shed light on the mechanism of gastric tumorigenesis.
A comparative structure model of splice variant 2 was computed based on its alignment to the known structure of cathepsin E intermediate (Protein Data Bank code 1TZS) and used to rationalize its conformational properties and loss of activity.
Emerging roles of cathepsin E in immune system cells and skin keratinocytes, and in host defense against cancer cells.
These results suggest the possible involvement of cathepsin E in disruption of the structural and functional integrity of alpha 2-macroglobulin (Montrer A2M Anticorps) in the endolysosome system.
Reduced expression of cathepsin E is observed in erythrocytes of humans with atopic dermatitis.
crystal structure of an activation intermediate of cathepsin E at 2.35A resolution
These results indicate that cathepsin E deficiency causes autophagy impairment concomitantly with increased aberrant mitochondria as well as increased oxidative stress.
impaired adipose tissue development in high fat diet-induced CatE(-/-) mice was probably due to reduced infiltration of macrophages and may lead to hepatomegaly accompanied by hepatic steatosis and hypercholesterolemia
L1 stimulation triggers sumoylation and cleavage of L1, thus generating the L1-70 fragment which is cleaved by cathepsin E
Intradermal cathepsin E has pruritogenic activity, which is at least partly mediated by the production of endothelin-1 (Montrer EDN1 Anticorps).
Low expression levels of MHC class II and cathepsin E might contribute to the defect in induction of Ag-specific T cells in NC mice.
Results suggest that Sp1 (Montrer SP1 Anticorps) binding plays a particularly important role in the regulation of cathepsin E gene expression.
the findings suggest that in keratinocytes CatE is functionally linked to the expression of terminal differentiation markers, thereby regulating epidermis formation and homeostasis.
Development of atopic dermatitis in cathepsin E-deficient mouse model is initiated by systemic accumulation of interleukin (IL)-18 (Montrer IL18 Anticorps) and IL-1 beta (Montrer IL1B Anticorps), mainly due to their reduced turnover rates.
Cathepsin E is expressed in mice myeloid dendritic cells, where it has an important nonredundant role in the class II major histocompatibility complex antigen processing pathway.
The protein encoded by this gene is a gastric aspartyl protease that functions as a disulfide-linked homodimer. This protease, which is a member of the peptidase C1 family, has a specificity similar to that of pepsin A and cathepsin D. It is an intracellular proteinase that does not appear to be involved in the digestion of dietary protein and is found in highest concentration in the surface of epithelial mucus-producing cells of the stomach. It is the first aspartic proteinase expressed in the fetal stomach and is found in more than half of gastric cancers. It appears, therefore, to be an oncofetal antigen. Transcript variants utilizing alternative polyadenylation signals and two transcript variants encoding different isoforms exist for this gene.
, erythrocyte membrane aspartic proteinase
, slow-moving proteinase
, procathepsin E