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Merck

49641

Sigma-Aldrich

乙醇脱氢酶,重组

≥500 U/mL

别名:

乙醇:NADP+ 氧化还原酶

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About This Item

CAS号:
MDL號碼:
分類程式碼代碼:
12352204
NACRES:
NA.54

重組細胞

expressed in E. coli

品質等級

形狀

liquid

比活性

≥500 U/mL

技術

cell based assay: suitable

顏色

light brownish-yellow to brown-green

適合性

suitable for molecular biology

應用

life science and biopharma

儲存溫度

−20°C

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一般說明

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。

應用

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。

生化/生理作用

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。

單位定義

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

象形圖

Exclamation mark

訊號詞

Warning

危險聲明

防範說明

危險分類

Eye Irrit. 2

儲存類別代碼

10 - Combustible liquids

水污染物質分類(WGK)

WGK 3

閃點(°F)

Not applicable

閃點(°C)

Not applicable

個人防護裝備

Eyeshields, Gloves


历史批次信息供参考:

分析证书(COA)

Lot/Batch Number

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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
H Eklund et al.
Biochemistry, 23(25), 5982-5996 (1984-12-04)
The binding of NAD to liver alcohol dehydrogenase has been studied in four different ternary complexes by using crystallographic methods. These complexes crystallize isomorphously in a triclinic crystal form which contains the whole dimer of the enzyme in the asymmetric
Tomáš Pluskal et al.
Nature plants, 5(8), 867-878 (2019-07-25)
Kava (Piper methysticum) is an ethnomedicinal shrub native to the Polynesian islands with well-established anxiolytic and analgesic properties. Its main psychoactive principles, kavalactones, form a unique class of polyketides that interact with the human central nervous system through mechanisms distinct
Albert Rosell et al.
Journal of molecular biology, 330(1), 75-85 (2003-06-24)
The amphibian enzyme ADH8, previously named class IV-like, is the only known vertebrate alcohol dehydrogenase (ADH) with specificity towards NADP(H). The three-dimensional structures of ADH8 and of the binary complex ADH8-NADP(+) have been now determined and refined to resolutions of

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