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Merck

N4505

Sigma-Aldrich

还原型 β-烟酰胺腺嘌呤二核苷酸 二钾盐

别名:

β-DPNH, β-NADH, DPNH, NADH, 二磷酸吡啶核苷酸,还原形式

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About This Item

线性分子式:
C21H27N7O14P2K2
分子量:
741.62
MDL编号:
UNSPSC代码:
41106305
PubChem化学物质编号:
NACRES:
NA.51

生物来源

synthetic

方案

≥95%

表单

powder

溶解性

10 mM NaOH: soluble-100 mg/mL, clear to hazy, faintly yellow to yellow

储存温度

−20°C

SMILES字符串

[K].NC(=O)C1=CN(C=CC1)C2OC(COP(O)(=O)OP(O)(=O)OCC3OC(C(O)C3O)n4cnc5c(N)ncnc45)C(O)C2O

InChI

1S/C21H29N7O14P2.K.H/c22-17-12-19(25-7-24-17)28(8-26-12)21-16(32)14(30)11(41-21)6-39-44(36,37)42-43(34,35)38-5-10-13(29)15(31)20(40-10)27-3-1-2-9(4-27)18(23)33;;/h1,3-4,7-8,10-11,13-16,20-21,29-32H,2,5-6H2,(H2,23,33)(H,34,35)(H,36,37)(H2,22,24,25);;

InChI key

KMRPNNQOKAHXEZ-UHFFFAOYSA-N

基因信息

human ... IMPDH2(3615)

应用

β-烟酰胺腺嘌呤二核苷酸(NAD +)和β-烟酰胺腺嘌呤二核苷酸还原(NADH)包含辅酶氧化还原对(NAD +:NADH),参与广泛的酶催化氧化还原反应。 除了其氧化还原功能外,NAD +/NADH是ADP-核糖基转移酶(ADP-核糖基转移酶;聚(ADP-核糖)聚合酶)反应中的ADP-核糖单元的供体和环状ADP-核糖(ADP-核糖基环化酶)的前体。

生化/生理作用

电子供体

储存分类代码

11 - Combustible Solids

WGK

WGK 3

闪点(°F)

Not applicable

闪点(°C)

Not applicable


历史批次信息供参考:

分析证书(COA)

Lot/Batch Number

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Nicotinamide adenine dinucleotide (NAD) is a coenzyme in metabolic reactions and cosubstrate in signaling pathways of cells. While the intracellular function of NAD is well described, much less is known about its importance as an extracellular molecule. Moreover, there is
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Scientific reports, 9(1), 19534-19534 (2019-12-22)
Metabolic profiles vary across all levels of biological diversity, from cells to taxa. Two-photon fluorescence lifetime imaging microscopy (FLIM) facilitates metabolic characterisation of biological specimens by assaying the intrinsic autofluorescence of the ubiquitous coenzymes NAD(P)H and FAD. The potential of
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The replication of chromosomes during S phase is critical for cellular and organismal function. Replicative stress can result in genome instability, which is a major driver of cancer. Yet how chromatin is made accessible during eukaryotic DNA synthesis is poorly
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Trypanosomatids possess glycosome organelles that contain much of the glycolytic machinery, including phosphofructokinase (PFK). We present kinetic and structural data for PFK from three human pathogenic trypanosomatids, illustrating intriguing differences that may reflect evolutionary adaptations to differing ecological niches. The

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