N0163
Nitrate Reductase from Arabidopsis thaliana
vial of ≥0.5 unit
Synonym(s):
NADH:nitrate oxidoreductase
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About This Item
Recommended Products
recombinant
expressed in Pichia pastoris
Quality Level
form
lyophilized powder
packaging
vial of ≥0.5 unit
shipped in
wet ice
storage temp.
−20°C
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Application
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 Actions
Nitrate reductase activity is induced in Arabidopsis thaliana plants by sumoylation via the E3 ligase activity of AtSIZ1.
Unit Definition
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.
Physical form
Supplied as a lyophilized powder containing 50 mM MOPS, pH 7.0, 0.1 mM EDTA and a proprietary sugar
Signal Word
Warning
Hazard Statements
Precautionary Statements
Hazard Classifications
Eye Irrit. 2 - Skin Irrit. 2 - STOT SE 3
Storage Class Code
11 - Combustible Solids
WGK
WGK 1
Flash Point(F)
Not applicable
Flash Point(C)
Not applicable
Personal Protective Equipment
dust mask type N95 (US), Eyeshields, Gloves
Certificates of Analysis (COA)
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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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