You Searched For: Fmoc-N-Me-Lys(boc)-OH

Supplier: Thermo Scientific Chemicals

Description: Applications: Extraction of metals

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Catalog Number: (89175-418)

Supplier: Labconco

Description: The regeneration plumbing connections to the 4% hydrogen/inert gas mixture, vacuum and vent. includes flexible tubing and fittings.

Catalog Number: (CAJT6906-2)

Supplier: AVANTOR PERFORMANCE MATERIAL LLC

Description: Water, ULTREX® II, Ultrapure, J.T.Baker®

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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: Thermo Scientific Chemicals

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

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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. 

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Catalog Number: (CA56621-930)

Supplier: 3M

Description: This respirator provides reliable worker protection against certain oil and non-oil based aerosols including those with nuisance levels of acid gases such as sulfur dioxide, hydrogen fluoride, and chlorine

Catalog Number: (10663-772)

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: (CAJT5367-03)

Supplier: AVANTOR PERFORMANCE MATERIAL LLC

Description: Hydrochloric acid 37% VLSI for microelectronic, J.T.Baker®

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Supplier: Thermo Scientific Chemicals

Description: A tracking dye for DNA sequencing

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Catalog Number: (10481-410)

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: (10481-406)

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: (76108-974)

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: (CA1.06587.1000)

Supplier: MilliporeSigma

Description: Buffer stock solution 1/15 mol/l

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Supplier: AVANTOR PERFORMANCE MATERIAL LLC

Description: Hydrochloric acid 37,0 - 38,0%, CMOS for microelectronic, J.T.Baker®

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Supplier: Honeywell Research Chemicals

Description: These buffer solutions are color-coded for easy identification and the pH 4 and 7 version have fungicide additive.

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