N1252
4-Nitrophenyl β-D-galactopyranoside
≥98% (enzymatic),≥98% (TLC), powder
别名:
p-Nitrophenyl β-D-galactopyranoside
产品名称
4-Nitrophenyl β-D-galactopyranoside, ≥98% (enzymatic)
方案
≥98% (TLC)
≥98% (enzymatic)
表单
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
储存分类代码
11 - Combustible Solids
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
涉药品监管产品
此项目有
历史批次信息供参考:
分析证书(COA)
Lot/Batch Number
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
Reuben E Huber et al.
Biochemistry, 42(6), 1796-1803 (2003-02-13)
Trp-999 is a key residue for the action of beta-galactosidases (Escherichia coli). Several site specific substitutions (Phe, Gly, Tyr, Leu) for Trp-999 were made. Each substitution caused greatly decreased affinities for substrates and inhibitors that bind in the "shallow" mode
Seçil Onal et al.
Artificial cells, blood substitutes, and immobilization biotechnology, 31(3), 339-355 (2003-08-09)
alpha-Galactosidase (alpha-D-galactoside galactohydrolase, EC 3.2.1.22) from watermelon was covalently immobilized on chitin. The immobilized alpha-galactosidase exhibited an activity of 0.61 U per g of carrier and an activity yield of 67%. The properties of free and immobilized alpha-galactosidase were also
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