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N3378

Sigma-Aldrich

4-Nitrophenyl β-D-fuco­pyran­oside

≥98% (TLC), powder

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25 MG
€61.20
100 MG
€141.00
1 G
€692.00

€61.20

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25 MG
€61.20
100 MG
€141.00
1 G
€692.00

About This Item

Empirical Formula (Hill Notation):
C12H15NO7
CAS Number:
1226-39-7
Molecular Weight:
285.25
Beilstein:
1291394
MDL number:
MFCD00040651
UNSPSC Code:
12352204
PubChem Substance ID:
24897639
NACRES:
NA.32

€61.20

Please contact Customer Service for Availability

Product Name

4-Nitrophenyl β-D-fuco­pyran­oside, ≥98% (TLC)

Assay

≥98% (TLC)

form

powder

solubility

ethanol: soluble 25 mg/mL, clear, colorless to faintly yellow

storage temp.

−20°C

SMILES string

C[C@H]1O[C@@H](Oc2ccc(cc2)[N+]([O-])=O)[C@H](O)[C@@H](O)[C@H]1O

InChI

1S/C12H15NO7/c1-6-9(14)10(15)11(16)12(19-6)20-8-4-2-7(3-5-8)13(17)18/h2-6,9-12,14-16H,1H3/t6-,9+,10+,11-,12+/m1/s1

InChI key

YILIDCGSXCGACV-BVWHHUJWSA-N

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Application

4-Nitrophenyl β-D-fucopyranoside has been used as a chromogenic substrate to study substrate specificity and kinetic parameters of β-galactosidase.[1][2][3]

Storage Class Code

11 - Combustible Solids

WGK

WGK 3

Flash Point(F)

Not applicable

Flash Point(C)

Not applicable

Personal Protective Equipment

dust mask type N95 (US), Eyeshields, Gloves

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Certificates of Analysis (COA)

Lot/Batch Number
SLCM9587
SLCN2161
SLCJ0021
SLCF8870
SLBX4599

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Identification, purification and characterization of a novel glycosidase (BgLm1) from Leuconostoc mesenteroides
del Pino-Garcia R, et al.
Food Sci. Technol., 122, 108829-108829 (2020)
New alkalophilic beta-galactosidase with high activity in alkaline pH region from Teratosphaeria acidotherma AIU BGA-1
Yamada M, et al.
Journal of Bioscience and Bioengineering, 123(1), 15-19 (2017)
Purification and analysis of an extremely halophilic beta-galactosidase from Haloferax alicantei
Holmes M L, et al.
Biochimica et Biophysica Acta, Protein Structure and Molecular Enzymology, 1337(2), 276-286 (1997)
Francisco de La Torre et al.
Plant physiology, 128(1), 247-255 (2002-01-15)
An alpha-L-fucosidase (EC 3.2.1.51) able to release the t-fucosyl residue from the side chain of xyloglucan oligosaccharides has been detected in the leaves of Arabidopsis plants. Moreover, an alpha-L-fucosidase with similar substrate specificity was purified from cabbage (Brassica oleracea) leaves
M H Tomassi et al.
Brazilian journal of medical and biological research = Revista brasileira de pesquisas medicas e biologicas, 43(1), 8-12 (2009-12-23)
The manner by which effects of simultaneous mutations combine to change enzymatic activity is not easily predictable because these effects are not always additive in a linear manner. Hence, the characterization of the effects of simultaneous mutations of amino acid
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