Glutaredoxin 1 Human Recombinant
Glutaredoxin 1 Yeast Recombinant
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.
Glutaredoxin 2 Yeast Recombinant
Glutaredoxin-3 Human Recombinant
Glutaredoxin 5 Human Recombinant
Glutaredoxin-2 E.Coli Recombinant
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 .
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 .
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 .
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 .
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 .
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 .
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 .