Technical Data
Glutathione Peroxidase 4 (GPX4, GPX-4, MCSP, Phospholipid Hydroperoxidase, Phospholipid Hydroperoxide Glutathione Peroxidase, Phospholipid Hydroperoxide Glutathione Peroxidase Mitochondrial, PHGPx, Sperm Nucleus Glutathione Peroxidase, snGPx, snPHGPx)
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.

Positive Control: Human Testis lysate
PabIgGAffinity Purified
100ug-20CBlue IceHumanGoat
Synthetic peptide, CEEPLVIEKDLPHY, representing the C Terminus of the human protein according to NP_002076.2; NP_001034937.1. Homology: Human
Purified by immunoaffinity chromatography.
Supplied as a liquid in Tris-saline, pH7.2, 0.5% BSA.
Species Crossreactivity: Human. Other species not tested.
Intended for research use only. Not for use in human, therapeutic, or diagnostic applications.
Su D, Novoselov SV, Sun QA, Moustafa ME, Zhou Y, Oko R, Hatfield DL, Gladyshev VN. Mammalian selenoprotein thioredoxin/glutathione reductase: Roles in disulfide bond formation and sperm maturation. J Biol Chem. 2005 May 18; [Epub ahead of print] PMID: 15901730