Oxidative Stress Enzymes Enzymes

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SRP0184 Aha1 Active human recombinant, expressed in E. coli, ≥90% (SDS-PAGE)  
SRP0181 AHCY Active human recombinant, expressed in E. coli, ≥90% (SDS-PAGE)  
C3155 Catalase from bovine liver aqueous solution, ≥30,000 units/mg protein Catalase catalyzes the degradation of hydrogen peroxide into water and oxygen. It can also react with alkylhydrogen peroxides, such as methylperoxide and ethylperoxide and the second H2O2 molecule can be replaced by methanol, ethanol, propanol, formate and nitrate as a hydrogen donor.
This product doesn′t need any activators, but it is inhibited by 3-amino-1-H-1,2,4 triazole, cyanide, azide, hydroxylamine, cyanogens bromide, 2-mercaptoethanol, dithiothreitol, dianisidnie and nitrate.
C100 Catalase from bovine liver aqueous suspension, 40,000-60,000 units/mg protein (E1%/405) Catalase catalyzes the degradation of hydrogen peroxide into water and oxygen. It can also react with alkylhydrogen peroxides, such as methylperoxide and ethylperoxide and the second H2O2 molecule can be replaced by methanol, ethanol, propanol, formate and nitrate as a hydrogen donor.
C5499 Cytochrome c Oxidase from bovine heart 5 mg protein/mL Cytochrome c oxidase is the principal terminal oxidase of high oxygen affinity in the aerobic metabolism of all animals, plants, yeasts and some bacteria. It is present in the mitochondria of the more highly developed cells and in the cytoplasmic membrane of bacteria. Cytochrome c oxidase catalyses the electron transfer from cytochrome c to O2. This electron-transfer process produces a proton gradient across the membrane, which in turn drives the production of ATP. This enzyme is unique in providing energy for the cell bycoupling the electron transport through the cytochrome chain with the process of oxidative phosphorylation.
G6137 Glutathione Peroxidase from bovine erythrocytes lyophilized powder, ≥300 units/mg protein Glutathione peroxidase is an enzyme which reduced lipid hydroperoxides into their corresponding alcohols. It also reduces free hydrogen peroxide in to water. In vivo it is responsible for protecting hemoglobin from oxidative breakdown.
Protects cells against oxidative damage by catalyzing the reduction of hydrogen peroxide in the presence of reducing agent glutathione. In cellular membranes it may induce lipid peroxidation through the reduction of hydrogen peroxide or polyunsaturated fatty acid hydroperoxides.
G4013 Glutathione Peroxidase from human erythrocytes lyophilized powder, ≥30 units/mg protein GPX1 (glutathione peroxidase 1) catalyzes the conversion of multiple organic and inorganic peroxides, by utilizing reduced glutathione (GSH) as an electron donor. This enzyme is also responsible for the removal of organic and inorganic peroxides.
SRP8010 GPX1 human recombinant, expressed in E. coli, His tagged, >90% (SDS-PAGE) GPX1 (glutathione peroxidase 1) is responsible for scavenging free radicals and derivatives. GPXs reduces lipid hydroperoxides to the corresponding alcohols as well as free hydrogen peroxide to water. Mutations in the GPX1 gene are associated with nonalcoholic fatty liver disease (NAFLD) susceptibility. Mutation in GPX1 at C594T is linked with oxidative stress-associated disorders, including prostate cancer and bladder cancer.
M6908 Myeloperoxidase from human leukocytes lyophilized powder, ≥50 units/mg protein Myeloperoxidase (MPO) has a crucial role to play in destruction of various microorganisms and foreign cells, such as bacteria, fungi, viruses, red cells and malignant and nonmalignant nucleated cells. MPO catalyzes the production of number of reactive oxidant species (ROS) that influence tissue damage during inflammation. MPO and its downstream inflammatory pathways function as a potent therapeutic target for prophylaxis of atherosclerotic cardiovascular disease. MPO catalyze the synthesis of polychlorinated dibenzo(p)dioxins and furans (PCDD/F) from precursor such as chlorophenols in presence of hydrogen peroxide (H2O2).
N0519 Nitrate Reductase (cytochrome) from Escherichia coli lyophilized powder, ≥5 units/g solid  
P8375 Peroxidase from horseradish Type VI, essentially salt-free, lyophilized powder, ≥250 units/mg solid (using pyrogallol) HRP readily combines with hydrogen peroxide (H2O2) and the resultant [HRP-H2O2] complex can oxidize a wide variety of hydrogen donors. The optimal pH is 6.0-6.5 and the enzyme is most stable in the pH range of 5.0-9.0. HRP can be conjugated to antibodies by several different methods including glutaraldehyde, periodate oxidation, through disulfide bonds, and also via amino and thiol directed cross-linkers. It is smaller and more stable than the enzyme labels β-galactosidase and alkaline phosphatase and hence, it is the most desired label. Also, its glycosylation leads to lower non-specific binding.
When incubated with a substrate, horseradish peroxidase produces a coloured, fluorimetric, or luminescent derivative of the labeled molecule, allowing quantification. Horseradish peroxidase has been shown to slightly reduce the level of inhibition in a cydAB mutant. Known inhibitors are sodium azide, cyanide, L-cystine, dichromate, ethylenethiourea, hydroxylamine, sulfide, vanadate, p-aminobenzoic acid, and Cd2+, Co2+, Cu2+, Fe3+, Mn2+, Ni2+, and Pb2+ ions.
P6782 Peroxidase from horseradish Type VI-A, essentially salt-free, lyophilized powder, 950-2000 units/mg solid (using ABTS), ≥250 units/mg solid (using pyrogallol) HRP readily combines with hydrogen peroxide (H2O2) and the resultant [HRP-H2O2] complex can oxidize a wide variety of hydrogen donors. The optimal pH is 6.0-6.5 and the enzyme is most stable in the pH range of 5.0-9.0. HRP can be conjugated to antibodies by several different methods that include the use of glutaraldehyde, periodate oxidation, disulfide bonds, and also via amino and thiol directed cross-linkers. It is smaller and more stable than the enzyme labels, β-galactosidase and alkaline phosphatase. Hence, it is the most desired label. Also, its glycosylation leads to lower non-specific binding. Sodium azide, cyanide, L-cystine, dichromate, ethylenethiourea, hydroxylamine, sulfide, vanadate, p-aminobenzoic acid, as well as Cd2+, Co2+, Cu2+, Fe3+, Mn2+, Ni2+, and Pb2+ ions are found to inhibit the enzyme activity.
When incubated with a substrate, horseradish peroxidase produces a coloured, fluorimetric, or luminescent derivative of the labeled molecule, allowing quantification. Horseradish peroxidase has been shown to slightly reduce the level of inhibition in a cydAB mutant.
P8986 Peroxiredoxin 1 human ≥85% (SDS-PAGE), recombinant, expressed in E. coli, lyophilized powder Peroxiredoxin 1 has a role in cellular peroxide scavenging and it modulates various signaling pathways. It is over-expressed in many cancer cells. It regulates cell growth and signaling by interacting with proteins like c-jun-N-terminal kinase and c-myc.
Peroxiredoxins are a novel defined family of peroxidases of approximately 25 kDa that reduce H2O2 and alkyl hydroperoxides and use mainly the thioredoxin (Trx) system (Trx, thioredoxin reductase and NADPH) as electron donor. The peroxiredoxin family includes more than 30 proteins from organisms of all kingdoms. Peroxiredoxin I belongs to the Type I Peroxiredoxin family. This family consists of human natural killer cell enhancing factor (NKEFA), human proliferation associated gene (PAG), mouse macrophage stress induced protein (MSP23), mouse osteoblast specific factor (OSF-3), and rat heme-binding protein (HBP23). These proteins share about 95% homology.
SRP0200 Peroxiredoxin I (K197Q) human recombinant, expressed in baculovirus infected insect cells, ≥80% (SDS-PAGE)  
SRP0201 Peroxiredoxin I (K197R) human recombinant, expressed in baculovirus infected insect cells, ≥90% (SDS-PAGE)  
SRP0202 Peroxiredoxin I Active human recombinant, expressed in baculovirus infected insect cells, ≥90% (SDS-PAGE)  
SRP0203 Peroxiredoxin II Active human recombinant, expressed in baculovirus infected insect cells, ≥80% (SDS-PAGE) Peroxiredoxin-2 is a ubiquitous redox-active intracellular enzyme that acts as a redox-dependent inflammatory mediator, triggering macrophages to produce and release TNF-α (tumor necrosis factor). It may be involved in peroxidase activity and resistance to overoxidation. Its levels are elevated in several human cancer cells and tissues, including colorectal cancer (CRC) and it influences diverse cellular processes involving cells survival, proliferation and apoptosis. Prdx2 plays an essential role in regulating oxidation-induced apoptosis in CRC cells and may have potential as a therapeutic target in CRC. It may also act as a possible candidate biomarker for pancreatic cancer. Prx2 is a key regulator of invasion and metastasis in melanoma.
SRP0249 PLK2 Active human recombinant, expressed in baculovirus infected insect cells, ≥60% (SDS-PAGE)  
SRP0250 PLK3 Active human recombinant, expressed in baculovirus infected insect cells, ≥80% (SDS-PAGE)  
S2515 Superoxide Dismutase from bovine erythrocytes lyophilized powder, 2,500-7,000 units/mg protein Catalyzes the dismutation of superoxide radicals to hydrogen peroxide and molecular oxygen. Plays a critical role in the defense of cells against the toxic effects of oxygen radicals. Competes with nitric oxide (NO) for superoxide anion (which reacts with NO to form peroxynitrite), thereby SOD promotes the activity of NO. SOD has also been shown to suppress apoptosis in cultured rat ovarian follicles, neural cell lines, and transgenic mice.
S5395 Superoxide Dismutase from bovine erythrocytes BioReagent, ≥3,000 units/mg protein, suitable for cell culture, lyophilized powder Catalyzes the dismutation of superoxide radicals to hydrogen peroxide and molecular oxygen. Plays a critical role in the defense of cells against the toxic effects of oxygen radicals. Competes with nitric oxide (NO) for superoxide anion (which reacts with NO to form peroxynitrite), thereby SOD promotes the activity of NO. SOD has also been shown to suppress apoptosis in cultured rat ovarian follicles, neural cell lines, and transgenic mice.
S7571 Superoxide Dismutase from bovine erythrocytes lyophilized powder, ≥3,000 units/mg protein Catalyzes the dismutation of superoxide radicals to hydrogen peroxide and molecular oxygen. Plays a critical role in the defense of cells against the toxic effects of oxygen radicals. Competes with nitric oxide (NO) for superoxide anion (which reacts with NO to form peroxynitrite), thereby SOD promotes the activity of NO. SOD has also been shown to suppress apoptosis in cultured rat ovarian follicles, neural cell lines, and transgenic mice.
S9636 Superoxide Dismutase from human erythrocytes essentially salt-free, lyophilized powder, ≥2,500 units/mg protein Catalyzes the dismutation of superoxide radicals to hydrogen peroxide and molecular oxygen. Plays a critical role in the defense of cells against the toxic effects of oxygen radicals. Competes with nitric oxide (NO) for superoxide anion (which reacts with NO to form peroxynitrite), thereby SOD promotes the activity of NO. SOD has also been shown to suppress apoptosis in cultured rat ovarian follicles, neural cell lines, and transgenic mice.
T7915 Thioredoxin Reductase from Escherichia coli ammonium sulfate suspension, >25 units/mg protein (Bradford) An FAD-containing enzyme involved in the transfer of hydrogen from E. coli thioredoxin to other proteins thus providing a powerful disulfide reductase system.
Thioredoxin reductase (TrxR) is an NADPH-dependent oxidoreductase containing one FAD per subunit that reduces the active site disulfide in oxidised thioredoxin (Trx). The molecular weight of the isozymes from mammalian sources vary between 55-67 kDa as compared with 35 kDa in prokaryotes, plants or yeast. The substrate specificity of the mammalian enzyme is much broader than the prokaryotic enzyme reducing both mammalian and E. coli thioredoxins as well as well as non-disulfide substrates such selenite, lipoic acids, lipid hydroperoxides and hydrogen peroxide.
Thioredoxin reductase is a FAD containing enzyme, which transfers the reducing equivalent from NADPH to the disulphide bond of the enzyme by using FAD moiety within the Cys-Ala-Thr-Cys sequence. It can also reduce Trx-S2 to Trx-(SH)2 by using NADPH.
T9698 Thioredoxin Reductase from rat liver buffered aqueous glycerol solution, ≥100 units/mg protein (Bradford) Thioredoxin reductase (TrxR) is a NADPH-dependent oxidoreductase containing one FAD per subunit that reduces the active site disulfide in oxidized thioredoxin (Trx). The molecular weight of the isozymes from mammalian sources vary between 55-67 kDa as compared with 35 kDa in prokaryotes, plants or yeast. The substrate specificity of the mammalian enzyme is much broader than the prokaryotic enzyme reducing both mammalian and E. coli thioredoxins as well as non-disulfide substrates such selenite, lipoic acids, lipid hydroperoxides, and hydrogen peroxide.
Thioredoxin reductase from mammalian sources contains a selenocysteine residue that is essential for the activity of the enzyme. It is one of the antioxidant enzymes present in the mammalian cell together with catalase, glutathione peroxidase and superoxide dismutase, and helps in removal of reactive oxygen species (ROS) from the cell. An example is the removal of excess nitric oxide (NO) by the formation of a complex with glutathione forming the S-nitroso-glutathione adduct (GS-NO). This can be cleaved directly by thioredoxin reductase. Hydrogen peroxide, another deleterious oxidant in the cell, is also reduced directly by mammalian TrxR.