Mouse Anti-GPX1 Recombinant Antibody (CBLG1-1668) (CBMAB-G4731-LY)

Glutathione Peroxidase 1

The protein encoded by this gene belongs to the glutathione peroxidase family, members of which catalyze the reduction of organic hydroperoxides and hydrogen peroxide (H2O2) by glutathione, and thereby protect cells against oxidative damage. Other studies indicate that H2O2 is also essential for growth-factor mediated signal transduction, mitochondrial function, and maintenance of thiol redox-balance; therefore, by limiting H2O2 accumulation, glutathione peroxidases are also involved in modulating these processes. Several isozymes of this gene family exist in vertebrates, which vary in cellular location and substrate specificity. This isozyme is the most abundant, is ubiquitously expressed and localized in the cytoplasm, and whose preferred substrate is hydrogen peroxide. It is also a selenoprotein, containing the rare amino acid selenocysteine (Sec) at its active site. Sec is encoded by the UGA codon, which normally signals translation termination. The 3' UTRs of selenoprotein mRNAs contain a conserved stem-loop structure, designated the Sec insertion sequence (SECIS) element, that is necessary for the recognition of UGA as a Sec codon, rather than as a stop signal. This gene contains an in-frame GCG trinucleotide repeat in the coding region, and three alleles with 4, 5 or 6 repeats have been found in the human population. The allele with 4 GCG repeats has been significantly associated with breast cancer risk in premenopausal women. Alternatively spliced transcript variants have been found for this gene. Pseudogenes of this locus have been identified on chromosomes X and 21. [provided by RefSeq, Aug 2017]

Protects the hemoglobin in erythrocytes from oxidative breakdown. In platelets, plays a crucial role of glutathione peroxidase in the arachidonic acid metabolism (PubMed:11115402).

Angiogenesis involved in wound healing Source: Ensembl
Arachidonic acid metabolic process Source: UniProtKB
Biological process involved in interaction with symbiont Source: Ensembl
Blood vessel endothelial cell migration Source: Ensembl
Cell redox homeostasis Source: BHF-UCL
Cellular response to oxidative stress Source: ParkinsonsUK-UCL
Endothelial cell development Source: Ensembl
Fat cell differentiation Source: Ensembl
Glutathione metabolic process Source: BHF-UCL
Heart contraction Source: BHF-UCL
Hydrogen peroxide catabolic process Source: BHF-UCL
Intrinsic apoptotic signaling pathway in response to oxidative stress Source: Ensembl
Lipoxygenase pathway Source: UniProtKB
Myoblast proliferation Source: Ensembl
Negative regulation of cysteine-type endopeptidase activity involved in apoptotic process Source: BHF-UCL
Negative regulation of extrinsic apoptotic signaling pathway via death domain receptors Source: BHF-UCL
Negative regulation of inflammatory response to antigenic stimulus Source: Ensembl
Negative regulation of oxidative stress-induced intrinsic apoptotic signaling pathway Source: Ensembl
Negative regulation of release of cytochrome c from mitochondria Source: BHF-UCL
Neuron apoptotic process Source: Ensembl
Positive regulation of protein kinase B signaling Source: Ensembl
Positive regulation of supramolecular fiber organization Source: ParkinsonsUK-UCL
Protein oxidation Source: Ensembl
Regulation of gene expression, epigenetic Source: BHF-UCL
Regulation of mammary gland epithelial cell proliferation Source: BHF-UCL
Regulation of proteasomal protein catabolic process Source: BHF-UCL
Response to gamma radiation Source: Ensembl
Response to hydrogen peroxide Source: BHF-UCL
Response to hydroperoxide Source: Ensembl
Response to selenium ion Source: BHF-UCL
Response to symbiotic bacterium Source: Ensembl
Response to xenobiotic stimulus Source: Ensembl
Sensory perception of sound Source: Ensembl
Skeletal muscle fiber development Source: Ensembl
Skeletal muscle tissue regeneration Source: Ensembl
Temperature homeostasis Source: Ensembl
Triglyceride metabolic process Source: Ensembl
UV protection Source: BHF-UCL
Vasodilation Source: Ensembl

Cytoplasm

During periods of oxidative stress, Sec-49 may react with a superoxide radical, irreversibly lose hydroselenide and be converted to dehydroalanine.