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the antioxidant enzyme GPX3 localizes to lung extracellular matrix and is variably upregulated in interstitial lung diseases.
These results suggest that GPx3 is an important factor for inhibition of Acetaminopheninduced hepatotoxicity both in vivo and in vitro.
GPX3 promoter methylation predicts colorectal carcinoma sensitivity to platinum.
Results indicate that selenoprotein P (Sepp1 (zeige SEPP1 Proteine)) is important for this transport in selenium-replete mice but that glutathione peroxidase-3 (Gpx3) is not.
GPx3 may have a possible role in modulating prostate carcinogenesis.
Sepp1 (zeige SEPP1 Proteine)(UF) and small selenium-containing proteins are filtered by the glomerulus and taken up by PCT (zeige UROD Proteine) cells via megalin (zeige LRP2 Proteine)-mediated endocytosis, preventing loss of selenium in the urine and providing selenium for the synthesis of glutathione peroxidase-3
GPX3 may play a major role in reducing hydrogen peroxide during decidualization.
Data indicate that uptake of Sepp1 (zeige SEPP1 Proteine) and Gpx3 by d-13 visceral yolk sac (zeige ADCY10 Proteine) was independent of apoER2 (zeige LRP8 Proteine) and megalin (zeige LRP2 Proteine).
an immunomodulatory role for GPX3 that limits the development of colitis-associated carcinoma.
We applied X-ray fluorescence microscopy to image selenium in mammalian tissues and identified a highly localized pool of this trace element at the basement membrane of kidneys that was associated with GPx3
GPX1, GPX3 and GPX4 may be upregulated in response to a change in oxidative stress during an acute coronary syndromes
An association of the GPX3-TNIP1 locus with ALS is identified using cross-ethnic meta-analyses. [Meta-Analysis]
Study provides evidence that GPX3 methylation in bone marrow is associated with adverse prognosis and leukemia transformation in myelodysplastic syndrome.
this paper shows that GPx3 expression can be regulated independently via epigenetic or glucocorticoid receptor (zeige NR3C1 Proteine)-mediated mechanisms in lung cancer cells
negative expression of GPX3 was related to poor prognosis in melanoma patients. These results suggest that methylation-mediated GPX3 repression may have critical implications for melanoma pathogenesis
The detection of the demethylated allele could be time and phe concentration dependent. The demethylated allele is suggested as an early epigenetic marker for an extracellular monitoring of an increased ROS production in newborns with PKU.
GPX1 (zeige GPX1 Proteine)*Pro198Leu AND GPX3 rs2070593 as genetic risk markers for Italian asthmatic patients
A three-way interaction among maternal and fetal variants in BHMT2 (zeige BHMT2 Proteine), GSTP1 (zeige GSTP1 Proteine) and GPX3 contribute to congenital heart defects
GPX3 hypermethylation is frequent in chronic myeloid leukemia (zeige BCL11A Proteine) and is negatively associated with its expression.
Exposure to follicular fluid transiently increased the transcript levels of IL8 (zeige IL8 Proteine) and PTGS2 (zeige PTGS2 Proteine), and decreased the expression of SOD2 (zeige SOD2 Proteine), GPX3, DAB2 (zeige DAB2 Proteine), and NR3C1 (zeige NR3C1 Proteine). TNF (zeige TNF Proteine) and IL6 (zeige IL6 Proteine) levels were also decreased while those of NAMPT (zeige NAMPT Proteine) were unaffected.
This gene product belongs to the glutathione peroxidase family, which functions in the detoxification of hydrogen peroxide. It contains a selenocysteine (Sec) residue at its active site. The selenocysteine is encoded by the UGA codon, which normally signals translation termination. The 3' UTR of Sec-containing genes have a common stem-loop structure, the sec insertion sequence (SECIS), which is necessary for the recognition of UGA as a Sec codon rather than as a stop signal.
glutathione peroxidase 3 (plasma)
, extracellular GPx
, plasma GPx
, plasma glutathione peroxidase
, extracellular glutathione peroxidase
, glutathione peroxidase 3