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anti-Human Glutathione Peroxidase 2 Antikörper:
anti-Mouse (Murine) Glutathione Peroxidase 2 Antikörper:
anti-Rat (Rattus) Glutathione Peroxidase 2 Antikörper:
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Human Polyclonal Glutathione Peroxidase 2 Primary Antibody für IHC, ELISA - ABIN250547
Esworthy, Yang, Frankel, Chu: Epithelium-specific glutathione peroxidase, Gpx2, is involved in the prevention of intestinal inflammation in selenium-deficient mice. in The Journal of nutrition 2005
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Human Polyclonal Glutathione Peroxidase 2 Primary Antibody für ELISA, WB - ABIN185424
McGrath-Morrow, Lauer, Yee, Neptune, Podowski, Thimmulappa, OReilly, Biswal: Nrf2 increases survival and attenuates alveolar growth inhibition in neonatal mice exposed to hyperoxia. in American journal of physiology. Lung cellular and molecular physiology 2009
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GPx2 may play an important role in the development of nasopharyngeal carcinoma. Furthermore, GPx2 may serve as a prognostic biomarker for NPC patient.
Yes associated protein 1 (YAP) activation led to excessive accumulation of reactive oxygen species (ROS) by downregulating the antioxidant enzyme glutathione peroxidase GPX2 in a manner related to tumor protein p63 blockade.
Results showed that the expression of GPX2 was significantly up-regulated within esophageal squamous cell carcinoma tissues.
Glutathione peroxidase 2 expression is a novel independent prognostic biomarker for gastric carcinoma that may be used to devise personalized therapeutic regimens and precision treatments for this disease
glutathione peroxidase 2 overexpression contributes to poor prognosis of hepatocellular carcinoma patients and helps to identify the high-risk hepatocellular carcinoma patients.
Cardamonin exposure and selenium availability regulate expression of HO-1, GPX2 and TrxR1 in human intestinal cells.
GPX2 underexpression is associated with advanced tumor status and implicated unfavorable clinical outcome of UCs, suggesting its role in tumor progression and may serve as a theranostic biomarker of UCs.
high GPx2 expression was associated with early tumor recurrence, particularly in the recently identified aggressive subtype of human colon cancer.
Patients with high GPX2 expression in biopsy specimen had significantly lower prostate-specific antigen recurrence-free survival and overall survival than those with no GPX2 expression.
miR-185 plays a role in up-regulation of GPX2 and SEPHS2 expression.
A role of GPx2, TrxR2 and TrxR3 in proliferation, apoptosis and, therefore, also during cancer development.
A GPx2-independent decrease in tumor development by selenium (Se) and detrimental effects of the Nrf2-activator sulforaphane in moderate Se deficiency.
Cellular and subcellular localization of gastrointestinal glutathione peroxidase in normal and malignant human intestinal tissue
Data suggest that some antioxidants may exert their anti-inflammatory and anticarcinogenic effects not only by induction of phase 2 enzymes but also by the up-regulation of the selenoprotein GI-GPx by Nrf2 binding.
some isoforms of p63 serve as a pro-survival factor by up-regulating GPX2 to reduce the p53-dependent oxidative stress-induced apoptotic response
Glutathione peroxidase 2 (GPX2) is the major oxidative stress-inducible cellular GPX isoform in the lungs, and its basal as well as inducible expression is dependent on Nrf2.
SNPs involving the GSTP1, MnSOD and GPX2 genes were not associated with Barrett's esophagus or esophageal adenocarcinoma
Activation of the glutathione peroxidase 2 (GPx2) promoter by beta-catenin.
Gpx2 is an overexpressed gene in human breast cancers
Results show that GPx2 by compartmentalized removal of hydroperoxides silences COX-2 activity and suppresses PGE(2)-dependent COX-2 and mPGES-1 expression.
The authors cloned cytosolic glutathione peroxidase (GPx1) and phospholipid hydroperoxide glutathione peroxidase (GPx4) genes in rainbow trout (Oncorhynchus mykiss). Constitutive mRNA expression and responsiveness to Se availability was analysed.
High glutathione peroxidase 2 expression is associated with radiation induced lung disease.
we propose that ileocolitis in the GPx1/2-double-knockout mice is caused by Nox1, which is induced by TNF
GPx2 is up-regulated in dysplastic colonic crypts, where it appears to act inhibit apoptosis and, thus, supports tumor development.
Candidate colitis genes in the Gdac1 locus of mice deficient in glutathione peroxidase-1 and -2, were analyzed.
it is concluded that GPx2, although supporting tumor growth, inhibits inflammation-mediated tumorigenesis, but the protective effect of selenium does not strictly depend on GPx2 expression
study indicates GI-GPx is spatiotemporally expressed in embryonic organs during organogenesis and may also perform a mutual compensatory role with cGPx in protecting embryos and extraembryonic tissues against reactive oxygen species
Loss of Gpx2 is associated with diet induced severe colitis.
In GPx2 KO mice, an increase in GPx1 can only partially compensate for GPx2, even under selenium supplementation, indicating that GPx2 is the major antiapoptotic GPx in the colon.
Genes encoding the antioxidants GPX2 and GSTO 1-1 are common inflammatory genes expressed upon induction of allergic airway inflammation, and independently of allergic susceptibility.
GPX1-DKO and GPX2-DKO mice are highly susceptible to bacteria-associated inflammation and cancer.
A trace amount of Gpx2 is protective against ileocolitis, and selenium and Gpx2 deficient mice will develop pathology similar to normal mice.
GPX2 activity is confined to the mucosal epithelium of the GI tract. Activity is detected all along the crypt-villus axis with concentration in the crypts. GPX1 activity is found in all layers of the gut and all parts of the mucosal epithelium.
Mice homozygous for combined targeted mutations of the Gpx1 and Gpx2 genes develop colitis at 11 days of age and ileitis by 21 days of age. This suggests that glutathione peroxidases function to prevent inflammation in the GI tract.
In the presence of normal microflora, mice deficient in Gpx1 and Gpx2 by targeted mutation develop ileocolitis at weaning. In the germfree state the mice display no GI tract pathology.
This gene is a member of the glutathione peroxidase family and encodes a selenium-dependent glutathione peroxidase that is one of two isoenzymes responsible for the majority of the glutathione-dependent hydrogen peroxide-reducing activity in the epithelium of the gastrointestinal tract. The protein encoded by this locus contains a selenocysteine (Sec) residue encoded by the UGA codon, which normally signals translation termination. Alternatively spliced transcript variants have been described.
gastrointestinal glutathione peroxidase
, glutathione peroxidase 2
, glutathione peroxidase-related protein 2
, glutathione peroxidase type 2
, glutathione peroxidase-gastrointestinal
, intestinal GPx