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Merck
CN

M7633

4-Methylumbelliferyl α-D-galactopyranoside

≥98% (TLC)

Synonym(s):

MU-alpha-GAL

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About This Item

Empirical Formula (Hill Notation):
C16H18O8
CAS Number:
38597-12-5
Molecular Weight:
338.31
UNSPSC Code:
12352204
NACRES:
NA.32
PubChem Substance ID:
24897170
EC Number:
254-031-1
Beilstein/REAXYS Number:
94674
MDL number:
MFCD00063278

Key Documents

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Product Name

4-Methylumbelliferyl α-D-galactopyranoside, ≥98% (TLC)

InChI key

YUDPTGPSBJVHCN-CHUNWDLHSA-N

InChI

1S/C16H18O8/c1-7-4-12(18)23-10-5-8(2-3-9(7)10)22-16-15(21)14(20)13(19)11(6-17)24-16/h2-5,11,13-17,19-21H,6H2,1H3/t11-,13+,14+,15-,16+/m1/s1

SMILES string

CC1=CC(=O)Oc2cc(O[C@H]3O[C@H](CO)[C@H](O)[C@H](O)[C@H]3O)ccc12

assay

≥98% (TLC)

form

powder

solubility

water: 50 mg/mL, clear, colorless to very faintly yellow

fluorescence

λex 317 nm; λem 374 nm (pH 9.1)
λex 360 nm; λem 449 nm (Reaction product)

storage temp.

−20°C

Quality Level

200

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Application

4-Methylumbelliferyl α-D-galactopyranoside has been used as an artificial substrate to assay α-galactosidase-A activity.

Biochem/physiol Actions

4-Methylumbelliferyl α-D-galactopyranoside is a fluorogenic substrate for α-galactosidase-A. The enzyme converts the substrate to form a blue fluorescent product, methylumbelliferyl. The fluorescence is measured spectrophotometrically.

Preparation Note

4-Methylumbelliferyl α-D-galactopyranoside is soluble in water (50 mg/ml), yielding a clear, colorless to faint yellow solution with the application of heat.

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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Certificates of Analysis (COA)

Lot/Batch Number
0000494410
0000494410
0000451365
0000451364
0000451364

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Zhen-Dan Shi et al.
Analytical and bioanalytical chemistry, 394(7), 1903-1909 (2009-06-13)
Alpha-galactosidase A hydrolyzes the terminal alpha-galactosyl moieties from glycolipids and glycoproteins in lysosomes. Mutations in alpha-galactosidase cause lysosomal accumulation of the glycosphingolipid, globotriaosylceramide, which leads to Fabry disease. Small-molecule chaperones that bind to mutant enzyme proteins and correct their misfolding
Eugènia Ruiz-Cánovas et al.
Colloids and surfaces. B, Biointerfaces, 208, 112123-112123 (2021-09-28)
The capability of HeLa cells to internalize large spherical microparticles has been evaluated by using inorganic, magnetic microparticles of 1 and 2.8 µm of diameter. In both absence but especially under the action of a magnet, both types of particles were
Nathaniel G Hentz et al.
Journal of laboratory automation, 19(2), 153-162 (2013-09-14)
This study illustrates how optimization of both liquid-handling accuracy and precision is critical to assay performance. The study was designed to examine (1) liquid-handling performance and (2) the effect of liquid-handling variability on two types of in vitro biochemical assays
Tali Kizhner et al.
Molecular genetics and metabolism, 114(2), 259-267 (2014-08-27)
Fabry disease is an X-linked recessive disorder caused by the loss of function of the lysosomal enzyme α-Galactosidase-A. Although two enzyme replacement therapies (ERTs) are commercially available, they may not effectively reverse some of the Fabry pathology. PRX-102 is a
Y Oda et al.
Analytical biochemistry, 254(1), 41-48 (1998-01-31)
A fluorometric assay of lectin binding to yeast cells is reported. The relative amount of biotinylated lectins bound to the yeast cells was estimated by enzyme activity using 4-methylumbelliferyl-beta-D-galactoside as a substrate for the lectin-bound beta-galactosidase through biotin-avidin interaction. Binding
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