推荐产品
质量水平
检测方案
≥98% (TLC)
≥98% (enzymatic)
形式
powder
溶解性
water: 10 mg/mL, clear, colorless to very faintly green
储存温度
−20°C
SMILES字符串
OC[C@H]1O[C@@H](Oc2ccc(cc2)[N+]([O-])=O)[C@H](O)[C@@H](O)[C@H]1O
InChI
1S/C12H15NO8/c14-5-8-9(15)10(16)11(17)12(21-8)20-7-3-1-6(2-4-7)13(18)19/h1-4,8-12,14-17H,5H2/t8-,9+,10+,11-,12-/m1/s1
InChI key
IFBHRQDFSNCLOZ-YBXAARCKSA-N
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应用
4-Nitrophenyl β-D-galactopyranoside has been used:
- as a substrate to assess the activity of glycosaminoglycan (GAG)-degrading enzymes
- as a substrate to study the kinetic properties of recombinant Leuconostoc mesenteroides glycosidase (BgLm1) and determine β-glucosidase activity
- to prepare substrate solution in a modified universal buffer
WGK
WGK 3
闪点(°F)
Not applicable
闪点(°C)
Not applicable
个人防护装备
Eyeshields, Gloves, type N95 (US)
法规信息
监管及禁止进口产品
Identification, purification and characterization of a novel glycosidase (BgLm1) from Leuconostoc mesenteroides
del Pino-Garcia R, et al.
LWT--Food Science and Technology null
A high-throughput microplate assay for simultaneous colorimetric quantification of multiple enzyme activities in soil
Popova IR and Deng S
Applied soil ecology : a section of Agriculture, Ecosystems & Environment null
Radosław Kowalewski et al.
Journal of vascular research, 43(1), 95-100 (2005-11-19)
The abdominal aortic aneurysm (AAA) wall represents an extreme example of arterial remodeling with disturbed elastin, collagen and proteoglycan metabolism. The aim of this study was to evaluate enzymes involved in the degradation of glycosaminoglycan chains and core proteins of
Daniel M Stoebel et al.
Genetics, 178(3), 1653-1660 (2008-02-05)
Transcriptional regulatory networks allow bacteria to express proteins only when they are needed. Adaptive hypotheses explaining the evolution of regulatory networks assume that unneeded expression is costly and therefore decreases fitness, but the proximate cause of this cost is not
Lan Guan et al.
Biochemistry, 42(6), 1377-1382 (2003-02-13)
Major determinants for substrate recognition by the lactose permease of Escherichia coli are at the interface between helices IV (Glu126, Ala122), V (Arg144, Cys148), and VIII (Glu269). We demonstrate here that Trp151, one turn of helix V removed from Cys148
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