方案
≥99.0% (GC)
表单
powder or crystals
mp
75-77 °C (lit.)
77-79 °C
储存温度
−20°C
SMILES字符串
CC(=O)Oc1ccc(cc1)[N+]([O-])=O
InChI
1S/C8H7NO4/c1-6(10)13-8-4-2-7(3-5-8)9(11)12/h2-5H,1H3
InChI key
QAUUDNIGJSLPSX-UHFFFAOYSA-N
基因信息
human ... PON1(5444)
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其他说明
Activated acetate; reagent for acetylations. Substrate for carboxy-esterase; Substrate for the determination of lipase
警示用语：
Danger
危险声明
危险分类
Eye Dam. 1 - Ox. Sol. 3 - Skin Sens. 1
储存分类代码
5.1B - Oxidizing hazardous materials
WGK
WGK 3
闪点(°F)
No data available
闪点(°C)
No data available
个人防护装备
Eyeshields, Gloves, type N95 (US)
法规信息
新产品
此项目有
Multiple forms of carboxylesterases in Baker's yeast.
E Parkkinen
Cellular and molecular biology, including cyto-enzymology, 26(2), 147-154 (1980-01-01)
Clemente Capasso et al.
Journal of enzyme inhibition and medicinal chemistry, 27(6), 892-897 (2012-07-19)
A new carbonic anhydrase (CA, EC 4.2.1.1) from the thermophilic bacterium Sulfurihydrogenibium yellowstonense YO3AOP1 was identified and characterized. The bacterial carbonic anhydrase gene was expressed in Escherichia coli yielding an active enzyme, which was purified in large amounts. The recombinant
Arna Runarsdottir et al.
Journal of molecular biology, 401(3), 451-464 (2010-07-06)
Glutathione transferases (GSTs) are known as promiscuous enzymes capable of catalyzing the conjugation of glutathione with a broad range of electrophilic substrates. A previous study based on recombinant chimeras derived from human GST M1-1 and GST M2-2 demonstrated the formation
E Björklund et al.
British journal of pharmacology, 161(7), 1512-1526 (2010-08-26)
Drugs used clinically usually have a primary mechanism of action, but additional effects on other biological targets can contribute to their effects. A potentially useful additional target is the endocannabinoid metabolizing enzyme monoacylglycerol lipase (MGL). We have screened a range
C S Wang
The Journal of biological chemistry, 256(19), 10198-10202 (1981-10-10)
Further studies on human milk bile salt-activated lipase were performed to provide kinetic and additional chemical characterizations of this enzyme. The enzyme was homogeneous by urea-sodium dodecyl sulfate-polyacrylamide gel electrophoresis and isoelectric focusing with an isoelectric point of 3.7. A
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