Product Details

Uniprot No.

Target Names

GLRX2

Alternative Names

bA101E13.1 (GRX2 glutaredoxin (thioltransferase) 2) antibody; bA101E13.1 antibody; CGI133 antibody; Glrx2 antibody; GLRX2_HUMAN antibody; Glutaredoxin-2 antibody; Glutaredoxin-2; mitochondrial antibody; GRX2 antibody; mitochondrial antibody

Raised in

Rabbit

Species Reactivity

Human,Mouse,Rat

Immunogen

Human GLRX2

Immunogen Species

Homo sapiens (Human)

Isotype

IgG

Purification Method

Antigen Affinity Purified

Concentration

It differs from different batches. Please contact us to confirm it.

Buffer

PBS with 0.02% Sodium Azide, 50% Glycerol, pH 7.3. -20°C, Avoid freeze / thaw cycles.

Tested Applications

ELISA,WB

Protocols

ELISA Protocol
Western Blotting(WB) Protocol

Troubleshooting and FAQs

Antibody FAQs

Storage

Upon receipt, store at -20°C or -80°C. Avoid repeated freeze.

Lead Time

Basically, we can dispatch the products out in 1-3 working days after receiving your orders. Delivery time maybe differs from different purchasing way or location, please kindly consult your local distributors for specific delivery time.

Target Background

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.

Gene References into Functions

GRX2 is important in the control of cardiac mitochondrial structure and function, and protects against human cardiac pathologies. PMID: 29101900
Study shows that Grx2 detoxifies *NO in mature oligodendrocytes and oligodendroglial precursor cellsvia the formation of dinitrosyl-iron-complexes, inhibiting the formation of harmful peroxynitrite and reducing subsequent oligodendroglial damage. Findings link inorganic biochemistry to neuroinflammation and identify glutaredoxin 2 as a protective factor against neuroinflammation-mediated myelin damage. PMID: 28618115
Grx2 and Trx1 contribute significantly to neuronal integrity and could be clinically relevant in neuronal damage following perinatal asphyxia and other neuronal disorders. PMID: 25735211
These results suggest that Grx2a plays proliferative and anti-apoptotic roles under serum deprivation. PMID: 21735102
Grx2 thiol redox regulation is essential for vertebrate embryonic development PMID: 22139372
Studies indicate that the mechanism of Grx2 protection against H(2)O(2)-induced apoptosis is likely associated with its ability to preserve complex I. PMID: 20547138
results suggest an important role for glutaredoxin 2 in protection and recovery from oxidative stress PMID: 14676218
Grx1 and Grx2 were present in placenta extracts and in cell lysates prepared from tumor cell lines; however, the levels of Grx1 were at least 20 times higher than those of Grx2; Grx2 was not detected in plasma from healthy blood donors PMID: 15184054
Lung cells can synthesize Grx2 mRNA and protein. PMID: 15297967
characterization of Grx2 as an iron-sulfur center-containing member of the thioredoxin fold protein family PMID: 15917333
Grx2 has a novel function as a peroxidase, accepting electrons both from GSH and TR. This unique property may play a role in protecting the mitochondria from oxidative damage. PMID: 17065220
The iron-sulfur cluster is complexed by the two N-terminal active site thiols of two Grx2 monomers and two molecules of glutathione that are bound noncovalently to the proteins and in equilibrium with glutathione in solution. PMID: 17115894
Eficence of an iron-sulfur cluster in which binding of the cluster inactivates the protein by sequestering active site residues and where loss of the cluster through changes in subcellular redox status creates a catalytically active protein. PMID: 17121859
Human Grx2 is found to be a conserved feature within the deuterostomes and appears to be the only additional conserved intramolecular disulfide within the glutaredoxins. PMID: 17546662
Grx2 is constitutively expressed in both neuron and glia in mouse and human brain including the neurons in human substantia nigra. PMID: 17961515
Grx1 and Grx2 exhibit key catalytic similarities, including selectivity for protein-SSG substrates and a nucleophilic, double-displacement, monothiol mechanism exhibiting a strong commitment to catalysis. PMID: 18816065
cluster signal of Grx2 is stable at positive potentials up to 0.5 V but that cluster destruction occurs readily when oxidative pulses in excess of this value are applied PMID: 19292455

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Subcellular Location

[Isoform 1]: Mitochondrion.; [Isoform 2]: Nucleus.

Protein Families

Glutaredoxin family

Tissue Specificity

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

Database Links

HGNC: 16065

OMIM: 606820

KEGG: hsa:51022

UniGene: Hs.458283