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Catalog Number: (PIER15169)
Supplier: Thermo Fisher Scientific
Description: QuantaBlu™ Fluorogenic peroxidase substrate kit is a three-component kit containing proprietary fluorescent substrate, peroxide and stop solutions for stopped (endpoint) or non-stopped assays.
UOM: 1 * 1 KIT

MSDS


Catalog Number: (BOSSBS-8300R-HRP)
Supplier: Bioss
Description: Peroxiredoxin (Prx) is an antioxidant enzyme detoxifying reactive oxygen species and has a cysteine at the active site. Prx enzymes modulate various receptor signaling pathways and protect cells from oxidatively induced death. Peroxiredoxin 1 to 4 have two conserved Cys residues corresponding to Cys51 and Cys172 of mammalian Peroxiredoxin 1. The active site cysteine(Cys51) is oxidized to cysteine sulfenic acid(Cys51-SOH) when a peroxide is reduced. Because Cys51-SOH is unstable, it forms a disulfide with Cys172-SH which comes from the other subunit of the homodimer. The disulfide is then reduced back to the Prx active thiol form by the thioredoxin-thioredoxin reductase system. However, the formation of the disulfide is a slow process. Thus under oxidative stress conditions, the sulfenic intermediate(Cys51-SOH) can be easily over oxidized to cysteine sulfinic acid(Cys-SO2H) or cysteine sulfonic acid(Cys-SO3H) before it is able to form a disulfide. Recent studies suggest that over oxidized Prx can be reduced back to the active form during recovery after oxidative stress.
UOM: 1 * 100 µl


Supplier: ENZO LIFE SCIENCES
Description: Heme Oxygenase-1 (HO-1) also known as Hsp32, is the inducible isoform of heme oxygenase that catalyzes the NADPH, oxygen, and cytochrome P450 reductase dependent oxidation of heme to carbon monoxide, ferrous iron and biliverdin which is rapidly reduced to bilirubin. These products of the HO reaction have important physiological effects: carbon monoxide is a potent vasodilator and has been implicated to be a physiological regulator of cGMP and vascular tone; biliverdin and its product bilirubin are potent antioxidants; "free" iron increases oxidative stress and regulates the expression of many mRNAs (e.g., DCT-1, ferritin and transferring receptor) by affecting the conformation of iron regulatory protein (IRP)-1 and its binding to iron regulatory elements (IREs) in the 5'- or 3'- UTRs of the mRNAs. To date, three identified heme oxygenase isoforms are part of the HO system that catalyze heme into biliverdin and carbon monoxide. These are inducible HO-1 or Hsp32, constitutive HO-2 that is abundant in the brain and testis, and HO-3 which is related to HO-2 but is the product of a different gene. The HO system is the rate-limiting step in heme degradation and HO activity decreases the levels of heme which is a well known potent catalyst of lipid peroxidation and oxygen radical formation.

Supplier: ENZO LIFE SCIENCES
Description: Heme Oxygenase-1 (HO-1) also known as Hsp32, is the inducible isoform of heme oxygenase that catalyzes the NADPH, oxygen, and cytochrome P450 reductase dependent oxidation of heme to carbon monoxide, ferrous iron and biliverdin which is rapidly reduced to bilirubin. These products of the HO reaction have important physiological effects: carbon monoxide is a potent vasodilator and has been implicated to be a physiological regulator of cGMP and vascular tone; biliverdin and its product bilirubin are potent antioxidants; "free" iron increases oxidative stress and regulates the expression of many mRNAs (e.g., DCT-1, ferritin and transferring receptor) by affecting the conformation of iron regulatory protein (IRP)-1 and its binding to iron regulatory elements (IREs) in the 5'- or 3'- UTRs of the mRNAs. To date, three identified heme oxygenase isoforms are part of the HO system that catalyze heme into biliverdin and carbon monoxide. These are inducible HO-1 or Hsp32, constitutive HO-2 that is abundant in the brain and testis, and HO-3 which is related to HO-2 but is the product of a different gene. The HO system is the rate-limiting step in heme degradation and HO activity decreases the levels of heme which is a well known potent catalyst of lipid peroxidation and oxygen radical formation.

Catalog Number: (USBI134382)
Supplier: US Biological
Description: Anti-TGFB1I1 Mouse Monoclonal Antibody [clone: 4B2-D8]
UOM: 1 * 100 µG


Catalog Number: (PRSI30-113)
Supplier: ProSci Inc.
Description: SOD1 binds copper and zinc ions and is one of two isozymes responsible for destroying free superoxide radicals in the body. This isozyme is a soluble cytoplasmic protein, acting as a homodimer to convert naturally-occuring but harmful superoxide radicals to molecular oxygen and hydrogen peroxide. The other isozyme is a mitochondrial protein. Mutations in its gene have been implicated as causes of familial amyotrophic lateral sclerosis.The protein encoded by this gene binds copper and zinc ions and is one of two isozymes responsible for destroying free superoxide radicals in the body. The encoded isozyme is a soluble cytoplasmic protein, acting as a homodimer to convert naturally-occuring but harmful superoxide radicals to molecular oxygen and hydrogen peroxide. The other isozyme is a mitochondrial protein. Mutations in this gene have been implicated as causes of familial amyotrophic lateral sclerosis. Rare transcript variants have been reported for this gene.
UOM: 1 * 100 µG


Catalog Number: (BOSSBS-8300R-A750)
Supplier: Bioss
Description: Peroxiredoxin (Prx) is an antioxidant enzyme detoxifying reactive oxygen species and has a cysteine at the active site. Prx enzymes modulate various receptor signaling pathways and protect cells from oxidatively induced death. Peroxiredoxin 1 to 4 have two conserved Cys residues corresponding to Cys51 and Cys172 of mammalian Peroxiredoxin 1. The active site cysteine(Cys51) is oxidised to cysteine sulfenic acid(Cys51-SOH) when a peroxide is reduced. Because Cys51-SOH is unstable, it forms a disulfide with Cys172-SH which comes from the other subunit of the homodimer. The disulfide is then reduced back to the Prx active thiol form by the thioredoxin-thioredoxin reductase system. However, the formation of the disulfide is a slow process. Thus under oxidative stress conditions, the sulfenic intermediate(Cys51-SOH) can be easily over oxidised to cysteine sulfinic acid(Cys-SO2H) or cysteine sulfonic acid(Cys-SO3H) before it is able to form a disulfide. Recent studies suggest that over oxidised Prx can be reduced back to the active form during recovery after oxidative stress.
UOM: 1 * 100 µl


Catalog Number: (VELTVEL101212S3016)
Supplier: VELTEK ASSOCIATES
Description: STERI-PEROX® wipes leave no residue and are used for both aseptic and non-aseptic wipe downs of filling and packaging machinery, stainless steel surfaces, Lexan, polycarbonate, glass, and any critical surfaces that require cleaning.
UOM: 1 * 200 items

Catalog Number: (BOSSBS-3896R-A750)
Supplier: Bioss
Description: Superoxide dismutase (SOD) is an antioxidant enzyme involved in the defence system against reactive oxygen species (ROS). SOD catalyses the dismutation reaction of superoxide radical anion (O2-) to hydrogen peroxide, which is then catalysed to innocuous O2 and H2O by glutathione peroxidase and catalase. Several classes of SOD have been identified. These include intracellular copper, zinc SOD (Cu, Zn-SOD/SOD-1), mitochondrial manganese SOD (Mn-SOD/SOD-2) and extracellular Cu, Zn-SOD (EC-SOD/SOD-3). SOD1 is found in all eukaryotic species as a homodimeric 32 kDa enzyme containing one each of Cu and Zn ion per subunit. The manganese containing 80 kDa tetrameric enzyme SOD2, is located in the mitochondrial matrix in close proximity to a primary endogenous source of superoxide, the mitochondrial respiratory chain. SOD3 is a heparin-binding multimer of disulfide-linked dimers, primarily expressed in human lungs, vessel walls and airways. SOD4 is a copper chaperone for superoxide dismutase (CCS), which specifically delivers Cu to copper/zinc superoxide dismutase. CCS may activate copper/zinc superoxide dismutase through direct insertion of the Cu cofactor.
UOM: 1 * 100 µl


Catalog Number: (MANA90728)
Supplier: MACHEREY-NAGEL
Description: This test paper allows the quick and easy detection of Cobalt (Co²⁺). For non-destructive testing of materials apply a drop of acid solution (50 ml hydrogen peroxide 3% + 7,5 ml O-phosphoric acid 85% + 5 ml hydrochloric acid 37 %) to the degreased surface.
UOM: 1 * 100 items

MSDS


Catalog Number: (STER6525M2EC)
Supplier: STERIS
Description: Spor-Klenz® Ready-To-Use Sterilants are fast acting, liquid sporicides specifically formulated for sterilization and disinfection of environmental, hard non-porous surfaces. Sterilants contain the proven blend of peracetic acid, hydrogen peroxide and acetic acid, that provides fast, effective microbial control of challenging spores such as <i>Bacillus subtilis</i> and <i>Bacillus cereus</i> and fungi like <i>Aspergillus brasiliensis.</i>
UOM: 1 * 4 items

Catalog Number: (AATB60012)
Supplier: AAT BIOQUEST
Description: Triton™ X-100 is a common non-ionic mild surfactant, which is often routinely utilized to lyse cells, extract proteins and cellular organelles, permeabilize the living cell membranes and solubilize proteins.
UOM: 1 * 50 mL


Catalog Number: (BOSSBS-12096R-FITC)
Supplier: Bioss
Description: Peroxisomes are single-membrane bound organelles present in virtually all eukaryotic cells. They are involved in numerous catabolic and anabolic pathways, including beta-oxidation of very long chain fatty acids, metabolism of hydrogen peroxide, plasmalogen biosynthesis and bile acid synthesis. The Peroxin gene family, which includes more than 20 members, is required for peroxisome biogenesis. Peroxin 5R, also known as PEX5-related protein or Peroxisome biogenesis factor 5-like, is a 626 amino acid protein that is mainly expressed in brain, with some expression in testis and pancreas. Peroxin 5R contains five TPR repeats, which enable protein-protein interactions and assembly of large multiprotein complexes. There are three isoforms of Peroxin 5R that are produced as a result of alternative splicing events. These isoforms bind C-terminal peroxisome-targeting signals in a similar manner to Peroxin-5. Peroxin 5R interacts with Rab 8b, possibly playing a role in vesicular trafficking and neurotransmitter release.
UOM: 1 * 100 µl


Catalog Number: (BOSSBS-12096R-A488)
Supplier: Bioss
Description: Peroxisomes are single-membrane bound organelles present in virtually all eukaryotic cells. They are involved in numerous catabolic and anabolic pathways, including beta-oxidation of very long chain fatty acids, metabolism of hydrogen peroxide, plasmalogen biosynthesis and bile acid synthesis. The Peroxin gene family, which includes more than 20 members, is required for peroxisome biogenesis. Peroxin 5R, also known as PEX5-related protein or Peroxisome biogenesis factor 5-like, is a 626 amino acid protein that is mainly expressed in brain, with some expression in testis and pancreas. Peroxin 5R contains five TPR repeats, which enable protein-protein interactions and assembly of large multiprotein complexes. There are three isoforms of Peroxin 5R that are produced as a result of alternative splicing events. These isoforms bind C-terminal peroxisome-targeting signals in a similar manner to Peroxin-5. Peroxin 5R interacts with Rab 8b, possibly playing a role in vesicular trafficking and neurotransmitter release.
UOM: 1 * 100 µl


Supplier: ENZO LIFE SCIENCES
Description: Heme Oxygenase-1 (HO-1) also known as Hsp32, is the inducible isoform of heme oxygenase that catalyzes the NADPH, oxygen, and cytochrome P450 reductase dependent oxidation of heme to carbon monoxide, ferrous iron and biliverdin which is rapidly reduced to bilirubin. These products of the HO reaction have important physiological effects: carbon monoxide is a potent vasodilator and has been implicated to be a physiological regulator of cGMP and vascular tone; biliverdin and its product bilirubin are potent antioxidants; "free" iron increases oxidative stress and regulates the expression of many mRNAs (e.g., DCT-1, ferritin and transferring receptor) by affecting the conformation of iron regulatory protein (IRP)-1 and its binding to iron regulatory elements (IREs) in the 5'- or 3'- UTRs of the mRNAs. To date, three identified heme oxygenase isoforms are part of the HO system that catalyze heme into biliverdin and carbon monoxide. These are inducible HO-1 or Hsp32, constitutive HO-2 that is abundant in the brain and testis, and HO-3 which is related to HO-2 but is the product of a different gene. The HO system is the rate-limiting step in heme degradation and HO activity decreases the levels of heme which is a well known potent catalyst of lipid peroxidation and oxygen radical formation.

Catalog Number: (BOSSBS-3896R-CY5.5)
Supplier: Bioss
Description: Superoxide dismutase (SOD) is an antioxidant enzyme involved in the defense system against reactive oxygen species (ROS). SOD catalyzes the dismutation reaction of superoxide radical anion (O2-) to hydrogen peroxide, which is then catalyzed to innocuous O2 and H2O by glutathione peroxidase and catalase. Several classes of SOD have been identified. These include intracellular copper, zinc SOD (Cu, Zn-SOD/SOD-1), mitochondrial manganese SOD (Mn-SOD/SOD-2) and extracellular Cu, Zn-SOD (EC-SOD/SOD-3). SOD1 is found in all eukaryotic species as a homodimeric 32 kDa enzyme containing one each of Cu and Zn ion per subunit. The manganese containing 80 kDa tetrameric enzyme SOD2, is located in the mitochondrial matrix in close proximity to a primary endogenous source of superoxide, the mitochondrial respiratory chain. SOD3 is a heparin-binding multimer of disulfide-linked dimers, primarily expressed in human lungs, vessel walls and airways. SOD4 is a copper chaperone for superoxide dismutase (CCS), which specifically delivers Cu to copper/zinc superoxide dismutase. CCS may activate copper/zinc superoxide dismutase through direct insertion of the Cu cofactor.
UOM: 1 * 100 µl


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Stock for this item is limited, but may be available in a warehouse close to you. Please make sure that you are logged in to the site so that available stock can be displayed. If the call is still displayed and you need assistance, please call us on +353 1 88 22222.
This product is marked as restricted and can only be purchased by approved Shipping Accounts. If you need further assistance, email VWR Regulatory Department at eurega_services@eu.vwr.com
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