You Searched For: Hydrogen+peroxide

Supplier: Thermo Scientific Chemicals

Description: Dihydrogen hexafluorotitanate 60% (w/w) in aqueous solution

Certificates

Catalog Number: (10481-414)

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: (10481-398)

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: (CA87003-236)

Supplier: BDH

Description: Ultra high-purity water for quantitative trace metal analysis in the parts-per-trillion (ppt) level.

SDS Certificates

Catalog Number: (76107-358)

Supplier: Bioss

Description: NHE-3 are integral membrane proteins that are expressed in most mammalian tissues, where they regulate intracellular pH and cell volume. NHEs mediate the transport of hydrogen (H+) ions out of cells in exchange for extracellular sodium (Na+) ions. While NHE-1 is ubiquitously expressed, the NHE isoforms 2-8 have distinct tissue- and cell type-dependent expression and inhibitory characteristics. NHE-3 localizes to the apical membrane of renal proximal tubules where it is responsible for most of the sodium transport and fluid reabsorption. NHE-3 translocates to internal pools where it mediates natriuresis when blood pressure increases abruptly. NHE-3 is also expressed in the stomach and functions to protect the mucosa by secreting protons that diffuse into the mucous cells.

Catalog Number: (CAJT5861-9)

Supplier: AVANTOR PERFORMANCE MATERIAL LLC

Certificates

Catalog Number: (10099-800)

Supplier: Prosci

Description: Organelles of the secretory and endocytic pathways are distinguished by their luminal acidity, which is generated by the activity of an electrogenic vacuolar-type hydrogen ATPase. Progressive acidification of vesicles in the endocytic pathway is essential for the redistribution and degradation of internalized membrane proteins, such as ligand receptor complexes and fluid-phase solutes. It may play an important role in maintaining cation homeostasis and function of the trans-Golgi network.Organelles of the secretory and endocytic pathways are distinguished by their luminal acidity, which is generated by the activity of an electrogenic vacuolar-type hydrogen ATPase. Progressive acidification of vesicles in the endocytic pathway is essential for the redistribution and degradation of internalized membrane proteins, such as ligand receptor complexes and fluid-phase solutes. This gene is expressed predominantly in the trans-Golgi network, and mediates the influx of sodium or potassium in exchange for hydrogen. It may thus play an important role in maintaining cation homeostasis and function of the trans-Golgi network. This gene is part of a gene cluster on chromosome Xp11.23.Organelles of the secretory and endocytic pathways are distinguished by their luminal acidity, which is generated by the activity of an electrogenic vacuolar-type hydrogen ATPase. Progressive acidification of vesicles in the endocytic pathway is essential for the redistribution and degradation of internalized membrane proteins, such as ligand receptor complexes and fluid-phase solutes. This gene is expressed predominantly in the trans-Golgi network, and mediates the influx of sodium or potassium in exchange for hydrogen. It may thus play an important role in maintaining cation homeostasis and function of the trans-Golgi network. This gene is part of a gene cluster on chromosome Xp11.23.

Catalog Number: (CA95022-238)

Supplier: HiMedia

Description: For the biochemical differentiation of <i>Salmonella</i> and <i>Shigella</i> species based on dextrose, lactose, sucrose fermentation, motility, hydrogen sulfide, indole, and urease production

SDS Certificates

Catalog Number: (CA1.07200.0105)

Supplier: MilliporeSigma

Description: Certipur grade, potassium hydrogen phthalate, directly traceable to primary SRM from NIST/PTB pH(S) = 4.005 (25 degree C).

SDS Certificates

Catalog Number: (TCD4214-250MG)

Supplier: TCI America

Description: 1,2-Distearoyl-sn-glycero-3-phosphoethanolamine, Purity: >97.0%(HPLC)(T), CAS Number: 1069-79-0, Molecular Formula: C41H82NO8P, MW: 748.08, Synonym: 2-Aminoethyl (R)-2,3-Bis(octadecanoyloxy)propyl Hydrogen Phosphate, DSPE, Size: 250MG

SDS

Supplier: VWR International

Description: J.T.Baker® volumetric and analytical solutions. These solutions are suitable for use in ACS, USP and NF compendial methods and general laboratory applications. 

Certificates

Supplier: Thermo Scientific Chemicals

Description: MDL: MFCD00013304

Certificates

Catalog Number: (75835-400)

Supplier: Restek

Description: Alkylation Derivatization Reagents

Catalog Number: (10481-412)

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: (76109-024)

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: (10481-402)

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.