GLRX1 Human

Glutaredoxin 1 Human Recombinant

Recombinant human Glutaredoxin, produced in E. coli, is a single, non-glycosylated polypeptide chain consisting of 106 amino acids. This protein has a molecular weight of 11.7 kDa.
Shipped with Ice Packs
Cat. No.
BT21767
Source
Escherichia Coli.
Appearance
This product appears as a clear, colorless solution that has been sterilized by filtration.

GLRX1 Yeast

Glutaredoxin 1 Yeast Recombinant

This product consists of the recombinant Glutaredoxin protein derived from Saccharomyces cerevisiae (Yeast). It has been engineered with a 6x His tag at the C-terminus and is produced in E. coli. The protein is a single, non-glycosylated polypeptide chain with a molecular weight of 16 kDa.
Shipped with Ice Packs
Cat. No.
BT21833
Source
Escherichia Coli.
Appearance
The product is a clear, colorless solution that has been sterilized by filtration.

GLRX2 Human

Glutaredoxin 2 Human Recombinant

Recombinant Human Glutaredoxin-2, expressed in E. coli, is a non-glycosylated polypeptide chain containing 154 amino acids (specifically, residues 20-164). This protein has a molecular weight of 17 kDa and includes a 9 amino acid His-tag fused at its C-terminus.
Shipped with Ice Packs
Cat. No.
BT21895
Source
Escherichia Coli.
Appearance
Clear, colorless, and sterile-filtered solution.

GLRX2 Yeast

Glutaredoxin 2 Yeast Recombinant

Recombinant Glutaredoxin-2 from Saccharomyces cerevisiae, engineered with a C-terminal 6x His tag, is produced in E. coli. This monomeric, non-glycosylated polypeptide has a molecular weight of 17 kDa.
Shipped with Ice Packs
Cat. No.
BT21972
Source
Escherichia Coli.
Appearance
A clear, colorless solution that has been sterilized through filtration.

GLRX3 Human

Glutaredoxin-3 Human Recombinant

Recombinant human GLRX3, produced in E. coli, is a single, non-glycosylated polypeptide chain consisting of 355 amino acids (residues 1-335) with a molecular weight of 39.6 kDa. The protein includes a 20 amino acid His Tag at the N-terminus and is purified using proprietary chromatographic methods.
Shipped with Ice Packs
Cat. No.
BT22024
Source
Escherichia Coli.
Appearance
A clear, colorless solution that has been sterilized by filtration.

GLRX5 Human

Glutaredoxin 5 Human Recombinant

Recombinant Human GLRX5, produced in E. coli, is a single, non-glycosylated polypeptide chain consisting of 177 amino acids (1-157 a.a.) with a molecular weight of 18.8 kDa. A 20 amino acid His Tag is fused to the N-terminus of GRX5, which is then purified using proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT22156
Source
Escherichia Coli.
Appearance
Clear, colorless, and sterile-filtered solution.

GRXB E.Coli

Glutaredoxin-2 E.Coli Recombinant

Produced in E. coli, GRXB is a single, non-glycosylated polypeptide chain comprising 235 amino acids (with amino acids 1-215 being of particular interest). It has a molecular weight of 26.5 kDa. For purification, GRXB is tagged with a 20 amino acid His-tag at the N-terminus and purified using proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT22232
Source
Escherichia Coli.
Appearance
A sterile, colorless solution free from particulate matter.
Definition and Classification

Glutaredoxins, also known as thioltransferases, are small redox enzymes that play a crucial role in maintaining cellular redox homeostasis. These enzymes, typically composed of approximately one hundred amino acids, utilize glutathione as a cofactor . Glutaredoxins are classified into several subfamilies based on their active sites, including the CPYC, CGFS, and CC subfamilies . The CPYC and CGFS subfamilies are present in eukaryotes, while the CC subfamily is exclusive to higher plants .

Biological Properties

Glutaredoxins are ubiquitously expressed across various organisms, including bacteria, plants, and animals . In humans, they participate in numerous cellular functions such as redox signaling and glucose metabolism regulation . These enzymes are distributed in various tissues, with specific isoforms localized to particular cellular compartments . For instance, in plants, glutaredoxins are involved in flower development and salicylic acid signaling .

Biological Functions

The primary biological function of glutaredoxins is to catalyze the reduction of disulfide bonds in proteins, thereby maintaining the redox state of the cell . They act as electron carriers in the glutathione-dependent synthesis of deoxyribonucleotides by ribonucleotide reductase . Additionally, glutaredoxins play a significant role in antioxidant defense by reducing dehydroascorbate, peroxiredoxins, and methionine sulfoxide reductase . In the immune system, they are involved in pathogen recognition and immune response modulation .

Modes of Action

Glutaredoxins function through interactions with other molecules and cells, primarily by catalyzing the reversible S-glutathionylation of proteins . This process involves the formation and reduction of mixed disulfides between glutathione and protein thiols, which can act as a regulatory switch for protein activity . Glutaredoxins also bind iron-sulfur clusters and deliver them to enzymes as needed . Their activity is closely linked to the glutathione system, where reduced glutathione regenerates oxidized glutaredoxins .

Regulatory Mechanisms

The expression and activity of glutaredoxins are tightly regulated at multiple levels. Transcriptional regulation involves various cis-regulatory elements responsive to environmental stimuli such as hormones and stress conditions . Post-translational modifications, including S-glutathionylation, also play a critical role in modulating glutaredoxin activity . These regulatory mechanisms ensure that glutaredoxins can respond dynamically to changes in cellular redox states and external stressors .

Applications

Glutaredoxins have significant applications in biomedical research, particularly in understanding redox biology and oxidative stress-related diseases . They are used as diagnostic tools to assess cellular redox states and as therapeutic targets for conditions such as cancer and cardiovascular diseases . In cancer research, glutaredoxins are studied for their role in modulating tumor growth, metastasis, and chemotherapy resistance . Additionally, small molecules that mimic glutaredoxin activity are being explored as potential therapeutic agents .

Role in the Life Cycle

Throughout the life cycle, glutaredoxins play essential roles in development, aging, and disease . In plants, they regulate growth and development processes and respond to environmental stimuli . In animals, glutaredoxins are involved in cellular differentiation, proliferation, and apoptosis . Their dysregulation is associated with various age-related diseases, including neurodegenerative disorders and cancer . Understanding the role of glutaredoxins in these processes provides insights into their potential as therapeutic targets for age-related diseases .

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