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GPX3 promoter methylation predicts colorectal carcinoma sensitivity to platinum.
Results indicate that selenoprotein P (Sepp1 (show SEPP1 Proteins)) 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 (show SEPP1 Proteins)(UF) and small selenium-containing proteins are filtered by the glomerulus and taken up by PCT (show UROD Proteins) cells via megalin (show LRP2 Proteins)-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 (show SEPP1 Proteins) and Gpx3 by d-13 visceral yolk sac (show ADCY10 Proteins) was independent of apoER2 (show LRP8 Proteins) and megalin (show LRP2 Proteins).
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
These results show that glutathione peroxidase 3 from the blood binds to basement membranes of specific epithelial cells and indicate that the cells modify their basement membranes to cause the binding.
GPx-3 deficiency results in a prothrombotic state and vascular dysfunction that promotes platelet-dependent arterial thrombosis
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 (show NR3C1 Proteins)-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 (show GPX1 Proteins)*Pro198Leu AND GPX3 rs2070593 as genetic risk markers for Italian asthmatic patients
A three-way interaction among maternal and fetal variants in BHMT2 (show BHMT2 Proteins), GSTP1 (show GSTP1 Proteins) and GPX3 contribute to congenital heart defects
GPX3 hypermethylation is frequent in chronic myeloid leukemia (show BCL11A Proteins) and is negatively associated with its expression.
Reduced GPX3 expression is associated with favorable/intermediate karyotypes but not with survival in de novo acute myeloid leukemia (show BCL11A Proteins) patients.
GPX1 (show GPX1 Proteins), GPX3, and GPX4 genes may play a role in clear cell renal cell carcinoma (show MOK Proteins) cancerogenesis.
Exposure to follicular fluid transiently increased the transcript levels of IL8 (show IL8 Proteins) and PTGS2 (show PTGS2 Proteins), and decreased the expression of SOD2 (show SOD2 Proteins), GPX3, DAB2 (show DAB2 Proteins), and NR3C1 (show NR3C1 Proteins). TNF (show TNF Proteins) and IL6 (show IL6 Proteins) levels were also decreased while those of NAMPT (show NAMPT Proteins) 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