G6673
Glutaredoxin-2 human
recombinant, expressed in E. coli, ≥90% (SDS-PAGE)
Synonym(s):
GLRX2, GRX2, TTase-2, Thiotransferase-2
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About This Item
UNSPSC Code:
12352200
NACRES:
NA.32
Recommended Products
recombinant
expressed in E. coli
assay
≥90% (SDS-PAGE)
form
buffered aqueous solution
specific activity
≥20 units/mg protein
UniProt accession no.
shipped in
dry ice
storage temp.
−20°C
Gene Information
human ... GLRX2(51022)
General description
Glutaredoxin-2 is a 15kDa mitochondrial thiol trasnferase that contains an N-terminal mitochondrial targeting signal. This protein is also composed of a CSYC (Cys-Ser-Tyr-Cys) motif.
Application
Glutaredoxin-2 (Grx2) human has been used as a supplement in reaction mixtures immediately before initiating Ogdh (2-oxoglutarate dehydrogenase) activity reaction, while performing Grx2 assay.
Biochem/physiol Actions
Glutaredoxin-2 catalyzes the disulfide formation and glutathionylation of proteins, especially complex I. This protein catalyzes reversible protein glutathionylation/deglutathionylation under varying range of GSH/GSSG ratios. Thus, it maintains the equilibrium between mitochondrial glutathione pool and protein thiols, thereby, regulating mitochondrial response to redox signals and oxidative stress.
Glutaredoxins (GRXs) participate in thio-disulfide exchange reactions in the presence of GSH, NADPH, and glutathione reductase. Glutaredoxins and thioredoxins belong to related families of low molecular mass enzymes that catalyze thio-disulfide exchange reactions. These enzymes are involved in electron transport, formation of disulfide linkage, protein folding, and protein regulation by thiol redox control.
Two Glutaredoxins have been identified in mammals:
Two Glutaredoxins have been identified in mammals:
- GRX1 is found in the cytosol and supplies ribonucleotide reductase with electrons. GRX! is involved in general disulfide-dithiol exchanges, dehydroascorbate reduction, cellular differentiation, regulation of transcription factors, and apoptosis.
- GRX2 plays a role in the cellular response to apoptotic stimuli and oxidative stress at the mitochondrial checkpoint. GRX2 has two isoforms (GRX2a and GRX2b) derived from alternative first exons. GRX2a is targeted to mitochondria; whereas, GRX2b is predicted to be localized in the nucleus. Unlike GRX1, GRX2 is not inhibited by oxidation of structural Cys residues. In addition, GRX2 can receive electrons not only from GSH, but also from thioredoxin reductase supporting both monothiol and dithiol reactions.
Unit Definition
1 unit oxidizes 1 μmole of NADPH per minute at pH 8 at 25 °C in a coupled reaction with glutathione reductase.
Physical form
Supplied as a solution in 10 mM MES buffer, pH 6.5, 1 mM EDTA, 1 mM DTT, and 100 mM NaCl.
Analysis Note
The product is the mature form of GRX2a, i.e. does not contain the mitochondria localization signal.
Storage Class
12 - Non Combustible Liquids
wgk_germany
WGK 2
flash_point_f
Not applicable
flash_point_c
Not applicable
Certificates of Analysis (COA)
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Elke Ströher et al.
Plant physiology, 170(3), 1284-1299 (2015-12-17)
Glutaredoxins (Grxs) are small proteins that function as oxidoreductases with roles in deglutathionylation of proteins, reduction of antioxidants, and assembly of iron-sulfur (Fe-S) cluster-containing enzymes. Which of the 33 Grxs in Arabidopsis (Arabidopsis thaliana) perform roles in Fe-S assembly in
Ryan J Mailloux et al.
Redox biology, 8, 285-297 (2016-03-02)
2-Oxoglutarate dehydrogenase (Ogdh) is an important mitochondria redox sensor that can undergo S-glutathionylation following an increase in H2O2 levels. Although S-glutathionylation is required to protect Ogdh from irreversible oxidation while simultaneously modulating its activity it remains unknown if glutathione can
Samantha M Beer et al.
The Journal of biological chemistry, 279(46), 47939-47951 (2004-09-07)
The redox poise of the mitochondrial glutathione pool is central in the response of mitochondria to oxidative damage and redox signaling, but the mechanisms are uncertain. One possibility is that the oxidation of glutathione (GSH) to glutathione disulfide (GSSG) and
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