Recombinant S. cerevisiae Glutaredoxin 1 protein is a Saccharomyces cerevisiae S288C Full Length protein, expressed in Escherichia coli, with >90% purity and suitable for FuncS.
| Application | Reactivity | Dilution info | Notes |
|---|---|---|---|
Application FuncS | Reactivity Reacts | Dilution info - | Notes Use at an assay dependent dilution. |
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Component of the glutathione system which performs several activities such as glutathione-dependent oxidoreductase, glutathione peroxidase and glutathione S-transferase (GST) activity (PubMed:11875065, PubMed:12684511). The disulfide bond functions as an electron carrier in the glutathione-dependent synthesis of deoxyribonucleotides by the enzyme ribonucleotide reductase. In addition, it is also involved in reducing cytosolic protein- and non-protein-disulfides in a coupled system with glutathione reductase. Required for resistance to reactive oxygen species (ROS) by directly reducing hydroperoxides and for the detoxification of ROS-mediated damage. GRX1 is less active as an oxidoreductase than GRX2 (PubMed:18992757, PubMed:20417731, PubMed:9571241).
Glutaredoxin 1
YCL035C, YCL35C, GRX1, Glutaredoxin-1, Glutathione-dependent oxidoreductase 1
Recombinant S. cerevisiae Glutaredoxin 1 protein is a Saccharomyces cerevisiae S288C Full Length protein, expressed in Escherichia coli, with >90% purity and suitable for FuncS.
Strongly binds to Glutathione, reduced and oxidized.
pH: 7.2 - 7.6
Preservative: 0.01% Sodium azide
Constituents: 0.395% Tris HCl
Component of the glutathione system which performs several activities such as glutathione-dependent oxidoreductase, glutathione peroxidase and glutathione S-transferase (GST) activity (PubMed:11875065, PubMed:12684511). The disulfide bond functions as an electron carrier in the glutathione-dependent synthesis of deoxyribonucleotides by the enzyme ribonucleotide reductase. In addition, it is also involved in reducing cytosolic protein- and non-protein-disulfides in a coupled system with glutathione reductase. Required for resistance to reactive oxygen species (ROS) by directly reducing hydroperoxides and for the detoxification of ROS-mediated damage. GRX1 is less active as an oxidoreductase than GRX2 (PubMed:18992757, PubMed:20417731, PubMed:9571241).
Belongs to the glutaredoxin family.
This product is an active protein and may elicit a biological response in vivo, handle with caution.
Glutaredoxin 1 also known as GLRX or thioltransferase is a small protein with a mass of around 12 kDa. It functions mechanically by catalyzing the reduction of disulfide bonds in proteins using glutathione as a cofactor. This enzyme plays a critical role in maintaining the redox balance within cells. Glutaredoxin 1 is widely expressed in various tissues with particularly high levels in the liver and brain. Its ubiquitous expression highlights its importance in cellular processes requiring reduction-oxidation reactions.
This enzyme acts as an important regulator in cellular redox homeostasis and defense against oxidative stress. Glutaredoxin 1 does not technically form a complex but often interacts with multiple other proteins to modulate their redox state. It is involved in the regulation of apoptosis signaling pathways and the repair of oxidatively damaged proteins. Through these actions Glutaredoxin 1 protects cells from damage and maintains proper cellular function.
Glutaredoxin 1 participates in key processes like the regulation of the thiol-disulfide balance and the glutathione metabolism pathway. These pathways are important for cellular detoxification and antioxidant defense. It works closely with glutathione peroxidase to mitigate oxidative damage and preserves cellular integrity by ensuring reduced forms of cysteine residues on proteins. This function links Glutaredoxin 1 to other proteins such as thioredoxin which shares similar roles in oxidative stress management.
Glutaredoxin 1 plays a significant part in neurodegenerative diseases and cardiovascular disorders. Its role in managing oxidative stress links it to conditions such as Alzheimer's disease where oxidative damage is a known contributor to disease progression. The relationship between Glutaredoxin 1 and proteins like amyloid-beta prevalent in Alzheimer's further highlights its importance. In cardiovascular disorders Glutaredoxin 1 influences the function of endothelial nitric oxide synthase a protein important for vascular health suggesting its involvement in maintaining vascular function and preventing cardiovascular diseases.
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