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Hydrogenperoxid 30%, Finyte® for microelectronic, J.T.Baker®

Varenummer: (5816-09)

Leverandør: Avantor

Beskrivelse: Hydrogenperoxid 30%, Finyte® for microelectronic, J.T.Baker®

UOM: 1 * 500 lb

Certifikater Tilbud

N/A Each

β-Thionicotinamide adenine dinucleotide, reduced form disodium salt ≥93.0% (by HPLC) for biochemical research

Varenummer: (TCIAT2980-100MG)

Leverandør: TCI

Beskrivelse: β-Thionicotinamide adenine dinucleotide, reduced form disodium salt ≥93.0% (by HPLC) for biochemical research

UOM: 1 * 100 mg

Tilbud

N/A Each

Dihydronicotinamidadenindinucleotiddinatrium salt (NADH-Na₂, reduceret form), Millipore®

Leverandør: Merck Millipore (Calbiochem‎)

Beskrivelse: Dihydronicotinamidadenindinucleotiddinatrium salt (NADH-Na₂, reduceret form), Millipore®

Nicotinamid-adenin dinucleotid (oxideret form) ≥98%, white powder cell culture reagent

Leverandør: MP Biomedicals

Beskrivelse: Storage: -20°C, desiccate
This is an ultrapure NAD, chromatographically purified to remove trace inhibitors.
β-NAD, a pyridine nucleotide and biologically active form of nicotinic acid, is a coenzyme necessary for the catalytic reaction of certain enzymes. It occurs in living cells primarily in the oxidized state. Serves as a coenzyme of the dehydrogenases, especially in the dehydrogenation of primary and secondary alcohols. NAD usually acts as a hydrogen acceptor, forming NADH which then serves as a hydrogen donor in the respiratory chain.
Many metabolites and enzymes of biological interest are present in tissues at low concentrations. With the use of β-NAD as a catalyst intermediate and several enzymes in a multistep system, known as enzyme cycling, much greater sensitivity for detection of these components is achieved. The reduced form, β-NADH, is fluorescent whereas β-NAD is not. This difference in fluorescence provides a sensitive fluorescent measurement of the oxidized or reduced pyridine nucleotides at concentrations down to 10-7 M.
Electron acceptor. β-NAD is a carrier for hydride ion, forming b-NADH. Hydride ion is enzymatically removed from a substrate molecule by the action of dehydrogenases such as malic dehydrogenase and lactic dehydrogenase. Such enzymes catalyze the reversible transfer of a hydride ion from malate or lactate to b-NAD to form the reduced product, b-NADH. Unlike b-NAD which has no absorbance at 340 nm, b-NADH absorbs at 340 nm (EmM = 6.22). The increase in absorbance at 340 nm with the formation of b-NADH is the basis for measurement of activity of many enzymes.