产品名称
乙醇脱氢酶，重组, ≥500 U/mL
recombinant
expressed in E. coli
form
liquid
specific activity
≥500 U/mL
technique(s)
cell based assay: suitable
color
light brownish-yellow to brown-green
suitability
suitable for molecular biology
application(s)
life science and biopharma
storage temp.
−20°C
Quality Level
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Application
醇脱氢酶（ADH）被用于逆转精神分裂症断裂基因1（DISC1-FL）和DB7细胞裂解物中缺乏的3-[4,5-二甲基噻唑-2-基]-2,5二苯基四唑溴化物（MTT）测定的减少。
Biochem/physiol Actions
醇脱氢酶催化醇氧化转化为醛。醇脱氢酶（ADH）催化的乙醇代谢引发活性氧（ROS）和一氧化氮（NO）的产生，导致线粒体和细胞蛋白氧化损伤，并进一步与神经炎症和神经系统疾病的发生有关。
General description
研究领域：神经科学
醇脱氢酶的同源二聚体结构在C端具有辅酶结合结构域，在N末端具有催化结构域。活动部位位于域间裂隙。NAD+在活性位点的结合会引起构象变化，从而形成醇底物的结合位点。
醇脱氢酶的同源二聚体结构在C端具有辅酶结合结构域，在N末端具有催化结构域。活动部位位于域间裂隙。NAD+在活性位点的结合会引起构象变化，从而形成醇底物的结合位点。
Other Notes
一个单位对应于在pH 7.0和30℃（NADPH作为辅助因子）下，每分钟减少1 μmol丙酮所需的酶量
signalword
Warning
hcodes
pcodes
Hazard Classifications
Eye Irrit. 2
存储类别
10 - Combustible liquids
wgk
WGK 3
flash_point_f
Not applicable
flash_point_c
Not applicable
ppe
Eyeshields, Gloves
法规信息
常规特殊物品
此项目有
Mechanism of alcohol-induced oxidative stress and neuronal injury
Haorah J, et al.
Free Radical Biology & Medicine, 45(11), 1542?1550-1542?1550 (2008)
Inhibition of protein translation by the DISC1-Boymaw fusion gene from a Scottish family with major psychiatric disorders
Ji B, et al.
Human Molecular Genetics, 23(21), 5683?5705-5683?5705 (2014)
Steven Hayward et al.
Biophysical journal, 91(5), 1823-1831 (2006-05-23)
Horse liver alcohol dehydrogenase is a homodimer, the protomer having a coenzyme-binding domain and a catalytic domain. Using all available x-ray structures and 50 ns of molecular dynamics simulations, we investigated the mechanism of NAD+-induced domain closure. When the well-known
Structure of a triclinic ternary complex of horse liver alcohol dehydrogenase at 2.9 A resolution.
H Eklund et al.
Journal of molecular biology, 146(4), 561-587 (1981-03-15)
F Colonna-Cesari et al.
The Journal of biological chemistry, 261(32), 15273-15280 (1986-11-15)
A study of the hinge bending mode in the enzyme liver alcohol dehydrogenase is made by use of empirical energy functions. The enzyme is a dimer, with each monomer composed of a coenzyme binding domain and a catalytic domain with
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