추천 제품
애플리케이션
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.
생화학적/생리학적 작용
Nitrate reductase activity is induced in Arabidopsis thaliana plants by sumoylation via the E3 ligase activity of AtSIZ1.
단위 정의
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.
물리적 형태
Supplied as a lyophilized powder containing 50 mM MOPS, pH 7.0, 0.1 mM EDTA and a proprietary sugar
신호어
Warning
유해 및 위험 성명서
예방조치 성명서
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
개인 보호 장비
dust mask type N95 (US), Eyeshields, Gloves
시험 성적서(COA)
제품의 로트/배치 번호를 입력하여 시험 성적서(COA)을 검색하십시오. 로트 및 배치 번호는 제품 라벨에 있는 ‘로트’ 또는 ‘배치’라는 용어 뒤에서 찾을 수 있습니다.
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)
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
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
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