Use your antibodies-online credentials, if available.
No Products on your Comparison List.
Your basket is empty.
Find out more
Glutathione is important for a variety of biological functions, including protection of cells from oxidative damage by free radicals, detoxification of xenobiotics, and membrane transport.
Showing 10 out of 22 products:
Redox-sensitive GFP revealed that gsh2 seedlings maintained redox poise in the cytoplasm but were more sensitive to oxidative challenge.
Mutation in glutathione synthetase gene impaired cadmium-induced sulfate assimilation.
Comparison of the pH profiles and the solvent deuterium isotope effects of A. thaliana glutathione synthetase and the Arg-132 and Arg-454 mutants suggest distinct mechanistic roles for these residues
Mutation in Glutathione Synthase gene is associated with chronic metabolic acidosis in glutathione synthetase deficiency.
Four SNPs (rs7265992, rs6060124, rs7260770, and rs4911455) in GSS were significantly associated with bladder cancer recurrence after transurethral resection and BCG (show SLC11A1 Proteins) treatment.
In this study, clinical, biochemical, and genetic aspects of five Chinese 5-oxoprolinuria patients with OPLAH (show OPLAH Proteins) or GSS gene mutations were investigated.
GCLC (show GCLC Proteins) and GSS were expressed at higher levels in colon cancer tissue, as compared with normal mucosa.
Studied the role of protein-protein interactions in the structural stability, activity and allostery of enzymes using the obligate homodimer human glutathione synthetase as an ideal model.
The findings indicate that Asp458 is essential for hGS catalysis and that it impacts the allostery of hGS.
These results imply that residues V44 and V45 are integral to the stability of human glutathione synthetase.
We have shown that susceptibility to health effects of air pollution on lung function growth is associated with genetic variation in the GSS gene
Single-nucleotide polymorphism in glutathione synthetase is associated with small-cell lung cancer.
This research indicates that Gly369 and Gly370 have essential roles in hGS, while Gly371 has a lesser involvement.
the cause of cellular ATP depletion in nephrotic cystinosis may be the futile cycle (show LRMP Proteins), formed between two ATP-dependant gamma-glutamyl cycle enzymes, gamma-glutamyl cysteine synthetase and 5-oxoprolinase (show OPLAH Proteins)
Hypoxia decreased 2 key enzyme activities that regulate GSH synthesis, glutamate cysteine ligase (GCL (show GCLC Proteins)) (E.C. 18.104.22.168) and glutathione synthase (GS) (E.C. 22.214.171.124)
PrP(c (show PRNP Proteins)) is expressed in all digestive regions of the rat, monkey, and cow; PrP(c (show PRNP Proteins)) expressing cells appeared scattered throughout the epithelium of fundic and pyloric glands as well as in intestinal villi and crypts.
Glutathione is important for a variety of biological functions, including protection of cells from oxidative damage by free radicals, detoxification of xenobiotics, and membrane transport. The protein encoded by this gene functions as a homodimer to catalyze the second step of glutathione biosynthesis, which is the ATP-dependent conversion of gamma-L-glutamyl-L-cysteine to glutathione. Defects in this gene are a cause of glutathione synthetase deficiency.
, GSH synthetase
, glutathione synthase
, glutathione synthetase, large subunit