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886 résultats pour « E1-ClipTip »

"E1-ClipTip"

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RECOM SERPIN E1 (PAI-1) CF 95% 25UG

Supplier: Biolegend

RECOM SERPIN E1 (PAI-1) CF 95% 25UG

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RECOM SERPIN E1 (PAI-1) CF 95% 10UG

Supplier: Biolegend

RECOM SERPIN E1 (PAI-1) CF 95% 10UG

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WEIGHT SET CLASS E1 W/NVLAP 13PC 1KG-1G

Supplier: Sartorius

WEIGHT SET CLASS E1 W/NVLAP 13PC 1KG-1G

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CLIPTIP 300 ART RACK ST PK960

CLIPTIP 300 ART RACK ST PK960

Supplier: Avantor

CLIPTIP 300 ART RACK ST PK960

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PIPETTOR F1 CLIPTIP 8 CHANNEL VOL-300 UL

Supplier: Thermo Fisher Scientific

PIPETTOR F1 CLIPTIP 8 CHANNEL VOL-300 UL

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ß-Nicotinamide adenine dinucleotide phosphate (NADP-Na2, oxidized form) ≥98%, white powder

Supplier: MP Biomedicals

β-NADP is a coenzyme necessary for the alcoholic fermentation of glucose and the oxidative dehydrogenation of other substances. It occurs widely in living tissue, especially in the liver. Nicotinic acid can be converted to nicotinamide in the body and, in this form, is found as a component of two oxidation-reduction coenzymes: nicotinamide adenine dinucleotide (NAD) and nicotinamide adenine dinucleotide phosphate (NADP). The nicotinamide portion of the coenzyme transfers hydrogens by alternating between oxidized quaternary nitrogen and a reduced tertiary nitrogen. NADP is an essential coenzyme for glucose-6-phosphate dehydrogenase which catalyzes the oxidation of glucose-6-phosphate to 6-phosphogluconic acid. This reaction initiates metabolism of glucose by a pathway other than the citric acid cycle. This route is known as the hexose phosphate shunt or phosphogluconate pathway. Other enzymes which utilize NADP as a coenzyme are: Alcohol dehydrogenase:NADP dependent; Aromatic ADH:NADP dependent; Ferredoxin-NADP reductase; L-Fucose dehydrogenase; Gabase; Galactose-1-phosphate uridyl transferase; Glucose dehydrogenase; L-Glutamic dehydrogenase; Glycerol dehydrogenase:NADP specific; Isocitric dehydrogenase; Malic enzymes; 5,10-Methylenetetrahydrofolate dehydrogenase; 6-Phosphogluconate dehydrogenase and Succinic semialdehyde dehydrogenase.

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