GLRX1 Human

Glutaredoxin 1 Human Recombinant

Glutaredoxin Human Recombinant produced in E.Coli is a single, non-glycosylated, Polypeptide chain containing 106 amino acids having a molecular mass of 11.7 kDa.
Shipped with Ice Packs
Cat. No.
BT21767
Source
Escherichia Coli.
Appearance
Sterile Filtered clear colorless solution.

GLRX1 Yeast

Glutaredoxin 1 Yeast Recombinant

Glutaredoxin Saccharamyces cerevisiae Recombinant containing 6x His tag at C-Terminus produced in E.Coli is a single, non-glycosylated, Polypeptide chain having a molecular mass of 16 kDa.
Shipped with Ice Packs
Cat. No.
BT21833
Source
Escherichia Coli.
Appearance
Sterile Filtered clear colorless solution.

GLRX2 Human

Glutaredoxin 2 Human Recombinant

Glutaredoxin-2 Human Recombinant produced in E.Coli is a single, non-glycosylated, Polypeptide chain containing 154 amino acids (20-164 a.a.) and having a molecular mass of 17 kDa. The GRX2 is fused to 9 amino acid His tag at C-Terminus.

Shipped with Ice Packs
Cat. No.
BT21895
Source
Escherichia Coli.
Appearance
Sterile Filtered clear colorless solution.

GLRX2 Yeast

Glutaredoxin 2 Yeast Recombinant

Glutaredoxin-2 Saccharamyces cerevisiae Recombinant containing 6x His tag at C-terminus produced in E.Coli is a single, non-glycosylated, Polypeptide chain having a molecular mass of 17 kDa.
Shipped with Ice Packs
Cat. No.
BT21972
Source
Escherichia Coli.
Appearance
Sterile Filtered clear colorless solution.

GLRX3 Human

Glutaredoxin-3 Human Recombinant

GLRX3 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 355 amino acids (1-335 a.a.) and having a molecular mass of 39.6kDa. GLRX3 is fused to a 20 amino acid His Tag at N-terminus and purified by proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT22024
Source
Escherichia Coli.
Appearance
Sterile filtered colorless solution.

GLRX5 Human

Glutaredoxin 5 Human Recombinant

GLRX5 Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 177 amino acids (1-157 a.a.) and having a molecular mass of 18.8 kDa. GRX5 is fused to a 20 amino acid His Tag at N-terminus and purified by proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT22156
Source
Escherichia Coli.
Appearance
Sterile filtered colorless solution.

GRXB E.Coli

Glutaredoxin-2 E.Coli Recombinant

GRXB produced in E.Coli is a single, non-glycosylated polypeptide chain containing 235 amino acids (1-215 a.a.) and having a molecular mass of 26.5kDa.
GRXB is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT22232
Source
Escherichia Coli.
Appearance
Sterile filtered colorless solution.
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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