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Wichtige Dokumente
N0163
Nitrate Reductase from Arabidopsis thaliana
vial of ≥0.5 unit
Synonym(e):
NADH:nitrate oxidoreductase
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About This Item
Empfohlene Produkte
Rekombinant
expressed in Pichia pastoris
Qualitätsniveau
Form
lyophilized powder
Verpackung
vial of ≥0.5 unit
Versandbedingung
wet ice
Lagertemp.
−20°C
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Anwendung
Nitrate reductase from Arabidopsis thaliana has been used in a study to assess the amino acid sequence of chicken hepatic sulfite oxidase.
Catalyzes the NADH-dependent reduction of nitrate to nitrite.
Biochem./physiol. Wirkung
Nitrate reductase activity is induced in Arabidopsis thaliana plants by sumoylation via the E3 ligase activity of AtSIZ1.
Einheitendefinition
One unit will reduce 1.0 micromole of nitrate to nitrite per min in a NADH system at pH 7.5 at 30 deg C.
Physikalische Form
Supplied as a lyophilized powder containing 50 mM MOPS, pH 7.0, 0.1 mM EDTA and a proprietary sugar
Signalwort
Warning
H-Sätze
P-Sätze
Gefahreneinstufungen
Eye Irrit. 2 - Skin Irrit. 2 - STOT SE 3
Lagerklassenschlüssel
11 - Combustible Solids
WGK
WGK 1
Flammpunkt (°F)
Not applicable
Flammpunkt (°C)
Not applicable
Persönliche Schutzausrüstung
dust mask type N95 (US), Eyeshields, Gloves
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Conserved domains in molybdenum hydroxylases. The amino acid sequence of chicken hepatic sulfite oxidase
The Journal of Biological Chemistry, 164, 20894-20901 (1989)
Arabidopsis nitrate reductase activity is stimulated by the E3 SUMO ligase AtSIZ1
Nature Communications, 19, 400-400 (2011)
Plant, cell & environment, 29(7), 1400-1409 (2006-11-04)
Temperature responses of nitrate reductase (NR) were studied in the psychrophilic unicellular alga, Koliella antarctica, and in the mesophilic species, Chlorella sorokiniana. Enzymes from both species were purified to near homogeneity by Blue Sepharose (Pharmacia, Uppsala, Sweden) affinity chromatography and
The Journal of biological chemistry, 276(29), 26995-27002 (2001-05-18)
Recombinant Arabidopsis NADH:nitrate reductase was expressed in Pichia pastoris using fermentation. Large enzyme quantities were purified for pre-steady-state kinetic analysis, which had not been done before with any eukaryotic nitrate reductase. Basic biochemical properties of recombinant nitrate reductase were similar
Journal of experimental botany, 53(370), 875-882 (2002-03-26)
The mechanism of the post-translational modulation of nitrate reductase activity (NR, EC 1.6.6.1) is briefly summarized, and it is shown that by this mechanism nitric oxide production through NR is also rapidly modulated. New and partly unexpected details on the
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