|Other Names||Glutaredoxin-2, mitochondrial, GLRX2, GRX2|
|Format||Synthetic peptide was lyophilized with 100% acetonitrile and is supplied as a powder. Reconstitute with 0.1 ml DI water for a final concentration of 1 mg/ml.|
|Storage||Maintain refrigerated at 2-8°C for up to 6 months. For long term storage store at -20°C.|
|Precautions||This product is for research use only. Not for use in diagnostic or therapeutic procedures.|
|Function||Glutathione-dependent oxidoreductase that facilitates the maintenance of mitochondrial redox homeostasis upon induction of apoptosis by oxidative stress. Involved in response to hydrogen peroxide and regulation of apoptosis caused by oxidative stress. Acts as a very efficient catalyst of monothiol reactions because of its high affinity for protein glutathione-mixed disulfides. Can receive electrons not only from glutathione (GSH), but also from thioredoxin reductase supporting both monothiol and dithiol reactions. Efficiently catalyzes both glutathionylation and deglutathionylation of mitochondrial complex I, which in turn regulates the superoxide production by the complex. Overexpression decreases the susceptibility to apoptosis and prevents loss of cardiolipin and cytochrome c release.|
|Cellular Location||Isoform 1: Mitochondrion.|
|Tissue Location||Widely expressed. Expressed in brain, heart, skeletal muscle, colon, thymus, spleen, kidney, liver, small intestine, placenta and lung. Not expressed in peripheral blood leukocytes.|
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Provided below are standard protocols that you may find useful for product applications.
Glutaredoxins (e.g., GLRX; MIM 600443) are a family ofglutathione-dependent hydrogen donors that participate in a varietyof cellular redox reactions.
Wu, H., et al. Biochim. Biophys. Acta 1797(10):1705-1715(2010)Mitra, S., et al. Biochemistry 48(18):3813-3815(2009)Gallogly, M.M., et al. Biochemistry 47(42):11144-11157(2008)Nagy, N., et al. J. Mol. Cell. Cardiol. 44(2):252-260(2008)Karunakaran, S., et al. Brain Res. 1185, 8-17 (2007) :
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