Recombinant Human GRX2 protein (His tag C-Terminus)
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(1 Publication)
Recombinant Human GRX2 protein (His tag C-Terminus) is a Human Full Length protein, expressed in Escherichia coli, with >90%, suitable for SDS-PAGE, Mass Spec.
View Alternative Names
GRX2, CGI-133, GLRX2
- SDS-PAGE
Supplier Data
SDS-PAGE - Recombinant Human GRX2 protein (His tag C-Terminus) (AB95471)
15% SDS-PAGE analysis of 3μg ab95471.
Reactivity data
Product details
Sequence info
Properties and storage information
Shipped at conditions
Appropriate short-term storage conditions
Appropriate long-term storage conditions
Aliquoting information
Storage information
Supplementary information
This supplementary information is collated from multiple sources and compiled automatically.
Biological function summary
The GRX2 protein plays a critical role in maintaining cellular redox balance by facilitating the reversible oxidation of protein cysteines. This is important for protecting cells against oxidative stress. GRX2 does not function as an isolated entity but instead forms part of larger multi-protein complexes interacting with other enzymes to regulate cellular homeostasis. These interactions help to protect cells from oxidative damage promote protein folding and regenerate other antioxidants.
Pathways
GRX2 holds a significant position in the redox regulation and antioxidant pathways. It partners with thioredoxin reductase and glutathione systems to mediate these pathways and manage cellular oxidative stress. The protein's activity is closely tied to glutathione with GRX2 often acting in synergy with glutathione to reduce complex oxidized protein thiols. This collaboration is vital in the oxidative stress response where the pathway elements must efficiently counterbalance oxidative challenges.
Specifications
Form
Liquid
Additional notes
ab95471 was purified by using conventional chromatography.
General info
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.
Sequence similarities
Belongs to the glutaredoxin family.
Subcellular localisation
Mitochondrion
Target data
Publications (1)
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Cell chemical biology 26:366-377.e12 PubMed30661989
2019
Applications
Unspecified application
Species
Unspecified reactive species
Product promise
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