A5298
3-Acetylpyridine hypoxanthine dinucleotide
~97%
登录 查看组织和合同定价。
选择尺寸
关于此项目
经验公式（希尔记法）:
C22H27N5O15P2
化学文摘社编号:
分子量:
663.42
NACRES:
NA.51
PubChem Substance ID:
UNSPSC Code:
41106305
MDL number:
Assay:
~97%
Form:
solid
Storage temp.:
−20°C
InChI
1S/C22H28N5O15P2/c1-10(28)11-3-2-4-26(5-11)21-17(31)15(29)12(40-21)6-38-43(34,35)42-44(36,37)39-7-13-16(30)18(32)22(41-13)27-9-25-14-19(27)23-8-24-20(14)33/h2-5,8-9,12-13,15-18,21-22,29-32H,6-7H2,1H3,(H,34,35)(H,36,37)(H,23,24,33)
SMILES string
CC(=O)C1=CC=C[N](=C1)C2OC(COP(O)(=O)OP(O)(=O)OCC3OC(C(O)C3O)n4cnc5C(=O)N=CNc45)C(O)C2O
InChI key
CRRQTCXZYOYDAM-UHFFFAOYSA-N
assay
~97%
form
solid
storage temp.
−20°C
正在寻找类似产品? 访问 产品对比指南
Application
3-Acetylpyridine hypoxanthine dinucleotide is an analogue of nicotinamide adenine dinucleotide (NAD) which may be used in mechanistic studies of NAD-dependent enzymes and enzymes that act upon NAD itself.
Other Notes
Analog of β-NAD
signalword
Warning
hcodes
Hazard Classifications
Eye Irrit. 2 - Skin Irrit. 2 - STOT SE 3
target_organs
Respiratory system
存储类别
11 - Combustible Solids
wgk
WGK 3
flash_point_f
Not applicable
flash_point_c
Not applicable
ppe
dust mask type N95 (US), Eyeshields, Gloves
法规信息
新产品
此项目有
G G Chang et al.
Archives of biochemistry and biophysics, 284(2), 285-291 (1991-02-01)
Initial velocity, product inhibition, and substrate inhibition studies suggest that the endogenous lactate dehydrogenase activity of duck epsilon-crystallin follows an order Bi-Bi sequential mechanism. In the forward reaction (pyruvate reduction), substrate inhibition by pyruvate was uncompetitive with inhibition constant of
H J Lee et al.
The Biochemical journal, 245(2), 407-414 (1987-07-15)
The structural requirements of the NADP+ molecule as a coenzyme in the oxidative decarboxylation reaction catalysed by pigeon liver malic enzyme were studied by kinetic and fluorimetric analyses with various NADP+ analogues and fragments. The substrate L-malate had little effect
T Gomi et al.
Biochimica et biophysica acta, 994(2), 172-179 (1989-02-02)
Rat liver S-adenosylhomocysteinase, a homotetramer, was resolved by treatment with acid ammonium sulfate into apoenzyme and NAD. The apoenzyme thus prepared retained a tetrameric structure but differed in the mobility on nondenaturing polyacrylamide gel electrophoresis. The inactive apoenzyme was reactivated
S L Oei et al.
FEBS letters, 397(1), 17-21 (1996-11-11)
Poly(ADP-ribosyl) transferase (pADPRT) catalyzes the transfer of the ADP-ribose moiety from NAD+ onto proteins as well as onto protein-bound ADP-ribose. As a result, protein-bound polymers of ADP-ribose are formed. pADPRT itself contains several acceptor sites for ADP-ribose polymers and may
我们的科学家团队拥有各种研究领域经验，包括生命科学、材料科学、化学合成、色谱、分析及许多其他领域.
联系客户支持