GLRX2 Antibody

1. GRX2 is important in the control of cardiac mitochondrial structure and function, and protects against human cardiac pathologies. PMID: 29101900
2. 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
3. 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
4. These results suggest that Grx2a plays proliferative and anti-apoptotic roles under serum deprivation. PMID: 21735102
5. Grx2 thiol redox regulation is essential for vertebrate embryonic development PMID: 22139372
6. 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
7. results suggest an important role for glutaredoxin 2 in protection and recovery from oxidative stress PMID: 14676218
8. 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
9. Lung cells can synthesize Grx2 mRNA and protein. PMID: 15297967
10. characterization of Grx2 as an iron-sulfur center-containing member of the thioredoxin fold protein family PMID: 15917333
11. 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
12. 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
13. 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
14. 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
15. Grx2 is constitutively expressed in both neuron and glia in mouse and human brain including the neurons in human substantia nigra. PMID: 17961515
16. 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
17. 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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HGNC: 16065

OMIM: 606820

KEGG: hsa:51022

UniGene: Hs.458283