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N3628

4-Nitrophenyl α-L-fuco­pyran­oside

≥98% (TLC), powder

Synonym(s):

4-Nitrophenyl alpha-L-fucopyranoside

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25 MG

$135.00

100 MG

$365.50

250 MG

$598.40

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$2,130.00

$135.00

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About This Item

Empirical Formula (Hill Notation):
C12H15NO7
CAS Number:
10231-84-2
Molecular Weight:
285.25
Beilstein/REAXYS Number:
89535
EC Number:
233-553-3
MDL number:
MFCD00063697
UNSPSC Code:
12352204
PubChem Substance ID:
24897654
NACRES:
NA.32

Key Documents

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Product Name

4-Nitrophenyl α-L-fuco­pyran­oside, ≥98% (TLC)

Quality Level

200

assay

≥98% (TLC)

form

powder

solubility

acetone: 4 mg/mL, clear, colorless

storage temp.

−20°C

SMILES string

C[C@@H]1O[C@@H](OCc2ccc(cc2)[N+]([O-])=O)[C@@H](O)[C@H](O)[C@@H]1O

InChI

1S/C13H17NO7/c1-7-10(15)11(16)12(17)13(21-7)20-6-8-2-4-9(5-3-8)14(18)19/h2-5,7,10-13,15-17H,6H2,1H3/t7-,10+,11+,12-,13+/m0/s1

InChI key

DCCILTHSDFBSCK-RCGNDRPLSA-N

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Show Differences

1 of 4

This Item
N0877N7763N3512
4-Nitrophenyl α-L-fuco­pyran­oside ≥98% (TLC)

Sigma-Aldrich

N3628

4-Nitrophenyl α-L-fuco­pyran­oside

4-Nitrophenyl α-D-galactopyranoside α-galactosidase substrate

Sigma-Aldrich

N0877

4-Nitrophenyl α-D-galactopyranoside

4-Nitrophenyl α-L-rhamnopyranoside powder

Sigma-Aldrich

N7763

4-Nitrophenyl α-L-rhamnopyranoside

4-Nitrophenyl α-L-arabinopyranoside arabinosidase substrate

Sigma-Aldrich

N3512

4-Nitrophenyl α-L-arabinopyranoside

assay

≥98% (TLC)

assay

≥99% (TLC)

assay

≥98% (TLC)

assay

≥98% (HPLC)

solubility

acetone: 4 mg/mL, clear, colorless

solubility

methanol: 100 mg/mL, clear to very slightly hazy

solubility

ethanol: soluble 49.00-51.00 mg/mL

solubility

ethanol: water (1:1): 19.60-20.40 mg/mL

Quality Level

200

Quality Level

200

Quality Level

200

Quality Level

200

form

powder

form

powder

form

powder

form

powder

storage temp.

−20°C

storage temp.

−20°C

storage temp.

−20°C

storage temp.

−20°C

Application

4-Nitrophenyl α-L-fucopyranoside (αfTM) has been used as a chemical substrate for α-fucosidase to determine carbohydrate-active enzymes (CAZymes) activity.[1] It has also been used as a nitrophenyl-linked substrate in p-nitrophenyl glycoside-based enzyme assays to determine the enzyme activity in cecal samples[2]

Biochem/physiol Actions

4-Nitrophenyl α-L-fucopyranoside is a chromogenic substrate that is used in kinetic studies of α-fucosidases.[3]

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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Certificates of Analysis (COA)

Lot/Batch Number
BCCN2904
BCCD0277
BCBN7349V
BCBL9273V
BCBJ6375V

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Alex Steimle et al.
STAR protocols, 2(1), 100326-100326 (2021-03-06)
The gut microbiome expresses a multitude of enzymes degrading polysaccharides in dietary plant fibers and in host-secreted mucus. The quantitative detection of these glycan-degrading enzymes in fecal samples is important to elucidate the functional activity of the microbiome in health
Mahesh S Desai et al.
Cell, 167(5), 1339-1353 (2016-11-20)
Despite the accepted health benefits of consuming dietary fiber, little is known about the mechanisms by which fiber deprivation impacts the gut microbiota and alters disease risk. Using a gnotobiotic mouse model, in which animals were colonized with a synthetic
Erik H Klontz et al.
Nature communications, 11(1), 6204-6204 (2020-12-06)
Fucosylation is important for the function of many proteins with biotechnical and medical applications. Alpha-fucosidases comprise a large enzyme family that recognizes fucosylated substrates with diverse α-linkages on these proteins. Lactobacillus casei produces an α-fucosidase, called AlfC, with specificity towards
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
View All Related Papers

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