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N1252

Sigma-Aldrich

4-Nitrophenyl β-D-galacto­pyran­oside

≥98% (enzymatic),≥98% (TLC), powder

Sinonimo/i:

p-Nitrophenyl β-D-galacto­pyran­oside

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About This Item

Formula empirica (notazione di Hill):
C12H15NO8
Numero CAS:
Peso molecolare:
301.25
Beilstein:
92213
Numero CE:
Numero MDL:
Codice UNSPSC:
12352204
ID PubChem:
NACRES:
NA.32

product name

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

Saggio

≥98% (TLC)
≥98% (enzymatic)

Forma fisica

powder

Solubilità

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

Temperatura di conservazione

−20°C

Stringa SMILE

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
IFBHRQDFSNCLOZ-YBXAARCKSA-N

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Applicazioni

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

Codice della classe di stoccaggio

11 - Combustible Solids

Classe di pericolosità dell'acqua (WGK)

WGK 3

Punto d’infiammabilità (°F)

Not applicable

Punto d’infiammabilità (°C)

Not applicable

Dispositivi di protezione individuale

Eyeshields, Gloves, type N95 (US)


Certificati d'analisi (COA)

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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
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
Hala Nehme et al.
Analytica chimica acta, 722, 127-135 (2012-03-27)
Enzymes are often quantified by measuring their biological activity. Capillary electrophoresis is gaining its position in this field due to the ongoing trend to miniaturize biochemical assays. The aim of this work was to compare pre-capillary (off-line) and in-capillary electrophoresis

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