N1252
4-Nitrophenyl β-D-galactopyranoside
≥98% (enzymatic),≥98% (TLC), powder
别名:
p-Nitrophenyl β-D-galactopyranoside
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关于此项目
经验公式（希尔记法）:
C12H15NO8
化学文摘社编号:
分子量:
301.25
NACRES:
NA.32
PubChem Substance ID:
UNSPSC Code:
12352204
EC Number:
221-584-5
MDL number:
Beilstein/REAXYS Number:
92213
产品名称
4-Nitrophenyl β-D-galactopyranoside, ≥98% (enzymatic)
InChI key
IFBHRQDFSNCLOZ-YBXAARCKSA-N
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
SMILES string
OC[C@H]1O[C@@H](Oc2ccc(cc2)[N+]([O-])=O)[C@H](O)[C@@H](O)[C@H]1O
assay
≥98% (TLC), ≥98% (enzymatic)
form
powder
solubility
water: 10 mg/mL, clear, colorless to very faintly green
storage temp.
−20°C
Quality Level
Application
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
存储类别
11 - Combustible Solids
wgk
WGK 3
flash_point_f
Not applicable
flash_point_c
Not applicable
ppe
Eyeshields, Gloves, type N95 (US)
法规信息
涉药品监管产品
此项目有
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
Chin-Pin Soh et al.
Phytochemistry, 67(3), 242-254 (2005-12-06)
alpha-Galactosidase (EC 3.2.1.22) from ripe papaya (Carica papaya L.) fruit was fractionated by a combination of ion exchange and gel filtration chromatography into three forms, viz., alpha-galactosidase 1, 2 and 3. The predominant isoform, alpha-gal 2, was probably a tetramer
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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