Enzymes
Product List
GLRX Mouse
Glutaredoxin Mouse Recombinant
GLRX Mouse Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 130 amino acids (1-107 a.a) and having a molecular mass of 14.3kDa. GLRX is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
PRDX2 Mouse
Eukaryotic Translation Initiation Factor 4E Mouse Recombinant
PRDX2 Mouse Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 222 amino acids (1-198 a.a) and having a molecular mass of 24.3kDa. PRDX2 is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
PRDX1 Human
Peroxiredoxin-1 Human Recombinant
The Peroxiredoxin is purified by proprietary chromatographic techniques.
PRDX1 Mouse
Peroxiredoxin-1 Mouse Recombinant
PRDX2 Human
Peroxiredoxin-2 Human Recombinant
The PRDX2 is purified by proprietary chromatographic techniques.
PRDX2 Rat
Peroxiredoxin-2 Rat Recombinant
PRDX3 Human
Peroxiredoxin-3 Human Recombinant
The PRDX3 is purified by proprietary chromatographic techniques.
PRDX4 Human
Peroxiredoxin-4 Human Recombinant
PRDX5 Human
Peroxiredoxin-5 Human Recombinant
The PRDX5 is purified by proprietary chromatographic techniques.
PRDX6 Human
Peroxiredoxin-6 Human Recombinant
The Peroxiredoxin-6 is purified by proprietary chromatographic techniques.
Introduction
Peroxiredoxins (Prxs) are a ubiquitous family of antioxidant enzymes that play a crucial role in reducing peroxides, such as hydrogen peroxide, alkyl hydroperoxides, and peroxynitrite . They are classified into six subgroups based on their structural and biochemical features: Prx1 (typical 2-Cys), Prx5, Prx6, PrxQ, Tpx, and AhpE . These enzymes are further categorized into 1-Cys and 2-Cys Prxs, depending on the number of cysteine residues involved in their catalytic mechanism .
Peroxiredoxins are highly abundant in various tissues and are expressed in different cellular compartments . They are particularly abundant in erythrocytes, where they play a significant role in protecting red blood cells from oxidative stress . The expression patterns of Prxs vary across different tissues, with some isoforms being more prevalent in specific organs . For example, Prx2 is one of the most abundant proteins in erythrocytes after hemoglobin .
The primary function of peroxiredoxins is to reduce peroxides, thereby protecting cells from oxidative damage . They also play a role in immune responses by modulating cytokine-induced peroxide levels . Additionally, Prxs are involved in pathogen recognition and defense mechanisms against infections . They act as molecular chaperones and participate in various signal transduction pathways .
Peroxiredoxins interact with other molecules and cells through their highly reactive cysteine residues . They form disulfide bonds with their binding partners, which are then reduced by thioredoxin or other reducing agents . This interaction leads to the activation of downstream signaling cascades that regulate various cellular processes . Prxs also act as molecular chaperones, protecting proteins from aggregation under stress conditions .
The expression and activity of peroxiredoxins are regulated at multiple levels. Transcriptional regulation involves various transcription factors that respond to oxidative stress . Post-translational modifications, such as phosphorylation, acetylation, and nitration, also play a significant role in modulating Prx activity . These modifications can alter the enzyme’s structure, localization, and interaction with other proteins .
Peroxiredoxins have several applications in biomedical research, including their use as biomarkers for oxidative stress and inflammation . They are also being explored as potential therapeutic targets for diseases associated with oxidative damage, such as cancer and neurodegenerative disorders . Additionally, Prxs are used in diagnostic tools to detect oxidative stress levels in various diseases .
Throughout the life cycle, peroxiredoxins play a vital role in maintaining cellular homeostasis . During development, they protect cells from oxidative damage and support proper cell differentiation and proliferation . In aging, Prxs help mitigate the effects of accumulated oxidative stress, thereby contributing to longevity . In disease states, such as cancer and neurodegenerative disorders, altered Prx expression and activity can impact disease progression and severity .
