Anti-Glutaredoxin-1 is produced in rabbit using as immunogen a human glutaredoxin-1 recombinant protein (G5298), conjugated to KLH. GRX1 is found in the cytosol and supplies ribonucleotide reductase with electrons.
Glutaredoxin-1 (Grx1) is encoded by the gene mapped to human chromosome 5q15. The encoded protein is a sulfhydryl disulfide oxidoreductase enzyme with a molecular mass of 12kDa. Grx1 belongs to the oxidoreductase family. Grx is expressed in various types of mammalian cells including human placenta and erythrocytes.
Immunogen
human glutaredoxin-1 recombinant protein conjugated to KLH
Application
Anti-Glutaredoxin-1 antibody produced in rabbit has been used in immunoblotting.
Biochem/physiol Actions
GRX1 is involved in general disulfide-dithiol exchanges, dehydroascorbate reduction and regulation of transcription factors.
Glutaredoxin (Grx) catalyzes glutathione (GSH)-dependent disulfide reductions when coupled to GSH, NADPH and glucocorticoid receptor (GR). Grx1 is implicated in various cellular processes, such as anti-oxidation, anti-apoptosis and regulation of cell differentiation. Additionally, the encoded protein also protects the retinal pigment epithelial (RPE) cells from H2O2-induced apoptosis by inhibiting protein kinase B (AKT) glutathionylation. Thus, Grx1 can be used as a potential therapeutic target for retinal degenerative diseases.
Physical form
Solution in 0.01 M phosphate buffered saline, pH 7.4, containing 15 mM sodium azide as a preservative
Disclaimer
Unless otherwise stated in our catalog or other company documentation accompanying the product(s), our products are intended for research use only and are not to be used for any other purpose, which includes but is not limited to, unauthorized commercial uses, in vitro diagnostic uses, ex vivo or in vivo therapeutic uses or any type of consumption or application to humans or animals.
Glutaredoxin 1 (GRX1) inhibits oxidative stress and apoptosis of chondrocytes by regulating CREB/HO-1 in osteoarthritis.
Sun J
Molecular Immunology, 211-218 (2017)
The thioredoxin and glutaredoxin systems are efficient electron donors to human plasma glutathione peroxidase.
Bjornstedt M
The Journal of Biological Chemistry, 269, 29382-29384 (1994)
Molecular mechanisms of thioredoxin and glutaredoxin as hydrogen donors for Mammalian s phase ribonucleotide reductase
Avval F, et al.
The Journal of Biological Chemistry, 284(13), 8233-8240 (2009)
Cloning, sequencing, and characterization of alternatively spliced glutaredoxin 1 cDNA and its genomic gene: chromosomal localization, mrna stability, and origin of pseudogenes.
Park JB and Levine M
The Journal of Biological Chemistry, 280, 10427-10434 (2005)
Characterization of human glutaredoxin 2 as iron-sulfur protein: a possible role as redox sensor
Lillig CH, et al.
Proceedings of the National Academy of Sciences of the USA, 102(23), 8168-8173 (2005)
Our team of scientists has experience in all areas of research including Life Science, Material Science, Chemical Synthesis, Chromatography, Analytical and many others.
