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May constitute a glutathione peroxidase-like protective system against oxidative stresses (By similarity). Additionally we are shipping GPX4 Antibodies (94) and GPX4 Proteins (10) and many more products for this protein.
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The proliferation of GPx4 siRNA-treated cells was downregulated compared with that of control siRNA-treated cells. GPx4 knockdown enhanced hydrogen peroxide- and ferrous sulfate-induced cytotoxicity.
High GPX4 expression is associated with oral squamous cell carcinoma.
By screening peptide libraries displayed on T7 phages, and analyzing the X-ray crystal structures of the peptides, we successfully identified one peptide that binds to near Sec73 of catalytic site and two peptides that bind to another site on GPX4. To our knowledge, this is the first study reporting GPX4 inhibitory peptides and their structural information.
use GPX4 and GPX7 (show GPX7 ELISA Kits) as possible markers for improving HCC (show FAM126A ELISA Kits) diagnosis/prognosis.
One SNP (rs3746162) in GPX4 was significantly associated with bladder cancer recurrence after transurethral resection.
Hepatitis C virus (HCV) induces oxidative stress but controls it tightly by inducing ROS scavengers. Among these, GPx4 plays an essential role in the HCV life cycle.
GPX1, GPX3, and GPX4 genes may play a role in clear cell renal cell carcinoma cancerogenesis.
polymorphism of gene of glutathione peroxidase (show GPX1 ELISA Kits) predisposes to more severe affection of liver and progression of chronic hepatitis C.
GPx4 is essential for maintaining oxidative homeostasis and keeping defense against oxidative stress in conjunctival epithelial cells.
Identification of truncating mutations in GPX4 in two families affected with Sedaghatian-type spondylometaphyseal dysplasia.
We found that the gpx4b gene shows maternal and zygotic gene expression in the embryo proper compared to gpx4a that showed zygotic gene expression in the periderm covering the yolk cell only.
The structure of the cytoplasmic isoform of mouse phospholipid hydroperoxide glutathione peroxidase (O70325-2 GPx4) with selenocysteine 46 mutated to cysteine is reported.
ferroptosis regulator Gpx4 is critical for hepatocyte survival and proper liver function, and that vitamin E can compensate for its loss by protecting cells against deleterious lipid peroxidation.
These data suggest that systemic inactivation of the Alox15 gene normalizes the reduced fertility of male Sec46Ala-Gpx4(+/-) mice by improving the motility of their sperm. If these data can be confirmed in humans, ALOX15 inhibitors might counteract male infertility related to GPX4 deficiency.
Phospholipid hydroperoxide glutathione peroxidase (show GPX1 ELISA Kits) is involved in the maintenance of male fertility under cryptorchidism in mice
dramatic motor neuron degeneration and paralysis induced by Gpx4 ablation suggest that ferroptosis inhibition by GPX4 is essential for motor neuron health and survival in vivo
The lack of catalytic activity is the major reason for the embryonic lethality of Gpx4 knockout mice.
Homozygous expression of Gpx4 with a targeted substitution of selenocysteine to serine causes early embryonic death as expected but, unexpectedly, male subfertility in heterozygous mice.
GPx4 suppresses the increase in the VEGF-A protein level, which occurs during the development of pathological CNV, thus partly explaining the protective effect of GPx4 against CNV.
Inducible disruption of Gpx4 causes acute renal failure and early death in an Alox15 (show ALOX15 ELISA Kits)-independent manner
A membrane glycoprotein GPX4 was shown to play a significant role in gamete interactions.
GPx-4 has an important role in the physiological control of peroxide tone in the bordering cells of the oviductal lumen
Glutathione peroxidase catalyzes the reduction of hydrogen peroxide, organic hydroperoxide, and lipid peroxides by reduced glutathione and functions in the protection of cells against oxidative damage. Human plasma glutathione peroxidase has been shown to be a selenium-containing enzyme and the UGA codon is translated into a selenocysteine. Through alternative splicing and transcription initiation, rat produces proteins that localize to the nucleus, mitochondrion, and cytoplasm. In humans, experimental evidence for alternative splicing exists\; alternative transcription initiation and the cleavage sites of the mitochondrial and nuclear transit peptides need to be experimentally verified.
, phospholipid hydroperoxide glutathione peroxidase, mitochondrial
, sperm nucleus glutathione peroxidase
, phospholipid hydroperoxide glutathione peroxidase, nuclear
, glutathione peroxidase 4
, sperm nuclei glutathione peroxidase
, glutathione peroxidase 4 (phospholipid hydroperoxidase)
, phospholipid hydroperoxide glutathione peroxidase