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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.
Catalog Number: BOSSBS-3896R-HRP
UOM: 1 * 100 µl
Supplier: Bioss


Description: Activity: 10 units/mg solid or more (containing approx. 20% of stabilisers). Unit definition: One unit causes the formation of one micromole of hydrogen peroxide per minute at pH 8,0 at 37 °C. Ref.: P.J.G. Mann and J.H. Quastel, Biochem. J., 31: 869 (1937)
Catalog Number: ICNA0215349280
UOM: 1 * 100 AU
Supplier: MP Biomedicals


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.
Catalog Number: BOSSBS-8300R-A350
UOM: 1 * 100 µl
Supplier: Bioss


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.
Catalog Number: PIER15169
UOM: 1 * 1 KIT
Supplier: Thermo Fisher Scientific

MSDS


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.
Catalog Number: BOSSBS-3896R-CY5
UOM: 1 * 100 µl
Supplier: Bioss


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


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.
Catalog Number: BOSSBS-12096R-FITC
UOM: 1 * 100 µl
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.
Catalog Number: BOSSBS-12096R-A488
UOM: 1 * 100 µl
Supplier: Bioss


Description: QuantaBlu™ NS/K Fluorogenic Substrate Kit is a two-component kit containing proprietary fluorescent substrate and peroxide solutions for non-stopped kinetic assays.
Catalog Number: PIER15162
UOM: 1 * 1 KIT
Supplier: Thermo Fisher Scientific


Description: Aldehyde dehydrogenase, dimeric NADP-preferring is an enzyme that in humans is encoded by the ALDH3A1 gene, belongs to the aldehyde dehydrogenase family. ALDHs play a major role in the detoxification of alcohol-derived acetaldehyde. They are involved in the metabolism of corticosteroids, biogenic amines, neurotransmitters, and lipid peroxidation. This protein preferentially oxidises aromatic aldehyde substrates. It may play a role in the oxidation of toxic aldehydes.
Catalog Number: PRSI92-459
UOM: 1 * 50 µG
Supplier: ProSci Inc.


Description: Capable of hydrolyzing lactones and a number of aromatic carboxylic acid esters. Has antioxidant activity. Is not associated with high density lipoprotein. Prevents LDL lipid peroxidation, reverses the oxidation of mildly oxidized LDL, and inhibits the ability of MM-LDL to induce monocyte chemotaxis.
Catalog Number: PRSI42-513
UOM: 1 * 100 µG
Supplier: ProSci Inc.


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.
Catalog Number: BOSSBS-8300R-A750
UOM: 1 * 100 µl
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.
Catalog Number: BOSSBS-8300R-A680
UOM: 1 * 100 µl
Supplier: Bioss


Description: Aldehyde dehydrogenases (ALDHs) mediate NADP+-dependent oxidation of aldehydes into acids during the detoxification of alcohol-derived acetaldehyde; metabolism of corticosteroids, biogenic amines and neurotransmitters; and lipid peroxidation. ALDH1A1, also designated retinal dehydrogenase 1 (RalDH1 or RALDH1), aldehyde dehydrogenase family 1 member A1, aldehyde dehydrogenase cytosolic, ALDHII, ALDH-E1 or ALDH E1, is a retinal dehydrogenase that participates in the biosynthesis of retinoic acid (RA). There are two major liver isoforms of ALDH1 that can localize to cytosolic or mitochondrial space. The ALDH1A2 (RALDH2, RALDH2-T) gene produces three different transcripts and also catalyzes the synthesis of RA from retinaldehyde. ALDH1A3 (ALDH6, RALDH3, ALDH1A6) is a 37 kb gene that consists of 13 exons and produces a major transcript of approximately 3.5 kb most abundant in salivary gland, stomach and kidney. ALDH3A1 (stomach type, ALDH3, ALDHIII) forms a cytoplasmic homodimer that preferentially oxidizes aromatic aldehyde substrates. ALDH genes upregulate as a part of the oxidative stress response, and appear to be abundant in certain tumors that have an accelerated metabolism toward chemotherapy agents.
Catalog Number: BOSSBS-12460R-HRP
UOM: 1 * 100 µl
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.
Catalog Number: BOSSBS-8300R-A488
UOM: 1 * 100 µl
Supplier: Bioss


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.
Catalog Number: AATB60012
UOM: 1 * 50 mL
Supplier: AAT BIOQUEST


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