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Merck
CN

N1252

4-Nitrophenyl β-D-galacto­pyran­oside

≥98% (enzymatic),≥98% (TLC), powder

Synonym(s):

p-Nitrophenyl β-D-galacto­pyran­oside

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About This Item

Empirical Formula (Hill Notation):
C12H15NO8
CAS Number:
Molecular Weight:
301.25
NACRES:
NA.32
PubChem Substance ID:
UNSPSC Code:
12352204
EC Number:
221-584-5
MDL number:
Beilstein/REAXYS Number:
92213
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Product Name

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

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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

Storage Class

11 - Combustible Solids

wgk

WGK 3

flash_point_f

Not applicable

flash_point_c

Not applicable

ppe

Eyeshields, Gloves, type N95 (US)

Regulatory Information

涉药品监管产品
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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
Identification, purification and characterization of a novel glycosidase (BgLm1) from Leuconostoc mesenteroides
del Pino-Garcia R, et al.
LWT--Food Science and Technology 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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