Anti-Glutaredoxin 2/GLRX2 Antibody Picoband® Fluoro647 Conjugated

GLRX2 (Glutaredoxin-2) also known as Glutaredoxin-2, mitochondrial or GRX2, is a protein that in humans is encoded by the GLRX2 gene. Glutaredoxins (e.g., GLRX) are a family of glutathione-dependent hydrogen donors that participate in a variety of cellular redox reactions. By sequence analysis, Lundberg et al. (2001) and Gladyshev et al. (2001) identified the GLRX2 gene within a clone mapping to chromosome 1q31.2-q31.3. Lundberg et al. (2001) determined that the GLRX2 gene contains 5 exons spanning about 9.6 kb. The GLRX2B transcript uses a first exon (exon 1B) located upstream from the first exon used by the GLRX2A transcript (exon 1A), suggesting that alternative splicing generates the isoforms. Lundberg et al. (2001) assayed reductase activity in recombinant proteins of both GLRX2 isoforms. They found that both have GSH-dependent dehydroascorbate reductase activity and 2-hydroxyethyl disulfide reductase activity.

A synthetic peptide corresponding to a sequence in the middle region of human Glutaredoxin 2, different from the related rat sequence by two amino acids, and from the related mouse sequence by one amino acid.

Widely expressed. Expressed in brain, heart, skeletal muscle, colon, thymus, spleen, kidney, liver, small intestine, placenta and lung. Not expressed in peripheral blood leukocytes. .

Cancer, Cell Biology, Metabolism, Mitochondrial, Mitochondrial Markers, Mitochondrial Metabolism, Oxidative Stress, Pathways and Processes, Redox Metabolism, Signal Transduction

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. .

1. Gladyshev, V. N., Liu, A., Novoselov, S. V., Krysan, K., Sun, Q.-A., Kryukov, V. M., Kryukov, G. V., Lou, M. F.Identification and characterization of a new mammalian glutaredoxin (thioltransferase), Grx2.J. Biol. Chem. 276: 30374-30380, 2001. 2. Lilig, C. H., Berndt, C., Vergnolle, O., Lonn, M. E., Hudemann, C., Bill, E., Holmgren, A.Characterization of human glutaredoxin 2 as iron-sulfur protein: a possible role as redox sensor.Proc. Nat. Acad. Sci. 102: 8168-8173, 2005. 3. Lundberg, M., Johansson, C., Chandra, J., Enoksson, M., Jacobsson, G., Ljung, J., Johansson, M., Holmgren, A.Cloning and expression of a novel human glutaredoxin (Grx2) with mitochondrial and nuclear isoforms.J. Biol. Chem. 276: 26269-26275, 2001.