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质量水平
表单
lyophilized
比活
≥175 μmole/min-mg (NADPH oxidized)
制造商/商品名称
Calbiochem®
储存条件
OK to freeze
技术
protein purification: suitable
NCBI登记号
运输
wet ice
储存温度
2-8°C
基因信息
Escherichia coli ... grxB(946926)
一般描述
Research area: CELL SIGNALING
Glutaredoxins (GRXs) are small thiol belonging to the Thioredoxin (TRX) superfamily. Different isoforms with varied functions have been identified in E.coli namely: glutaredoxin 1, glutaredoxin 2, and glutaredoxin 3. Native glutaredoxin-S2 isolated from E. coli. Glutaredoxin functions as a glutathione-dependent hydrogen donor for ribonucleotide reductase. It is useful as a general disulfide reductant for the in vitro study of protein folding mechanisms and has been demonstrated to work in conjunction with protein disulfide isomerase to enhance refolding of scrambled RNase A and RNase T1.
Glutaredoxins (GRXs) are small thiol belonging to the Thioredoxin (TRX) superfamily. Different isoforms with varied functions have been identified in E.coli namely: glutaredoxin 1, glutaredoxin 2, and glutaredoxin 3. Native glutaredoxin-S2 isolated from E. coli. Glutaredoxin functions as a glutathione-dependent hydrogen donor for ribonucleotide reductase. It is useful as a general disulfide reductant for the in vitro study of protein folding mechanisms and has been demonstrated to work in conjunction with protein disulfide isomerase to enhance refolding of scrambled RNase A and RNase T1.
应用
Glutaredoxin-S2 has been used:
- to catalyze the reduction of S-glutathionylated cysteine residues, to facilitate the detection of protein S-glutathionylation in FFPE HLTF-/-CDX sections.
- for reduction of the protein sulfhydryl groups that were modified by glutathione for subsequent labeling and purification of glutathionylated mitochondrial proteins.
生化/生理作用
Glutaredoxins (Grxs) are a group of small redox proteins that play crucial roles in maintaining iron-sulfur metabolism and cellular redox homeostasis. These proteins function as thioltransferases , dehydroascorbate reductases, and transhydrogenases. They also participate in de-nitrosylation reactions and contribute to the conversion of cystine. Additionally, GRX2 plays a key role in neural and cardiac development. Low levels of GRX2 transcripts in humans may lead to conditions such as fibrosis, hypertrophy, and infarctions of the left ventricle.
警告
Toxicity: Standard Handling (A)
单位定义
Units are defined using a standard HED assay.
外形
Lyophilized from 0.5% NH₄HCO₃.
重悬
Reconstitute in 1 ml 50 mM Tris-HCl, 1 mM EDTA, pH 7.5 to yield a final concentration of 1 mg/ml.
其他说明
Ruoppolo, M., et al. 1997. Biochemistry36, 12259.
Sun, C., et al. 1997. Protein Sci.6, 383.
Prinz, W.A., et al. 1997. J. Biol. Chem.272, 15661.
Holmgren, A. and Alund, F. 1995 Methods Enzymol.252, 283.
Hoog, J.O., et al. 1986. Gene43, 13.
Sun, C., et al. 1997. Protein Sci.6, 383.
Prinz, W.A., et al. 1997. J. Biol. Chem.272, 15661.
Holmgren, A. and Alund, F. 1995 Methods Enzymol.252, 283.
Hoog, J.O., et al. 1986. Gene43, 13.
法律信息
CALBIOCHEM is a registered trademark of Merck KGaA, Darmstadt, Germany
储存分类代码
11 - Combustible Solids
WGK
WGK 1
闪点(°F)
Not applicable
闪点(°C)
Not applicable
The adaptive metabolic response involves specific protein glutathionylation during the filamentation process in the pathogen Candida albicans
Gergondey R, et al.
Biochimica et Biophysica Acta, 1862(7), 1309-1323 (2016)
Modulation of the specific glutathionylation of mitochondrial proteins in the yeast Saccharomyces cerevisiae under basal and stress conditions
Gergondey R, et al.
The Biochemical Journal, 474(7), 1175-1193 (2017)
Helicase-like transcription factor (HLTF)-deleted CDX/TME model of colorectal cancer increased transcription of oxidative phosphorylation genes and diverted glycolysis to boost S-glutathionylation in lymphatic intravascular metastatic niches
Martinez-Marin D, et al.
PLoS ONE, 18(9), e0291023-e0291023 (2023)
Glutaredoxin.
A Holmgren et al.
Methods in enzymology, 252, 283-292 (1995-01-01)
C Sun et al.
Protein science : a publication of the Protein Society, 6(2), 383-390 (1997-02-01)
Human glutaredoxin is a member of the glutaredoxin family, which is characterized by a glutathione binding site and a redox-active dithiol/disulfide in the active site. Unlike Escherichia coli glutaredoxin-1, this protein has additional cysteine residues that have been suggested to
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