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N1252

Sigma-Aldrich

4-Nitrophenyl β-D-galacto­pyran­oside

≥98% (enzymatic),≥98% (TLC), powder

Sinónimos:

p-Nitrophenyl β-D-galacto­pyran­oside

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About This Item

Fórmula empírica (notación de Hill):
C12H15NO8
Número de CAS:
3150-24-1
Peso molecular:
301.25
Beilstein/REAXYS Number:
92213
EC Number:
221-584-5
MDL number:
MFCD00063256
UNSPSC Code:
12352204
PubChem Substance ID:
24897472
NACRES:
NA.32

product name

4-Nitrophenyl β-D-galacto­pyran­oside, ≥98% (enzymatic)

Quality Level

300

assay

≥98% (TLC)
≥98% (enzymatic)

form

powder

solubility

water: 10 mg/mL, clear, colorless to very faintly green

storage temp.

−20°C

SMILES string

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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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_germany

WGK 3

flash_point_f

Not applicable

flash_point_c

Not applicable

ppe

Eyeshields, Gloves, type N95 (US)

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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
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
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