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N0877

Sigma-Aldrich

4-Nitrophenyl α-D-galactopyranoside

α-glucosidase substrate, chromogenic, ≥99% (TLC), powder

Synonym(s):

p-Nitrophenyl α-D-galactopyranoside

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About This Item

Empirical Formula (Hill Notation):
C12H15NO8
CAS Number:
Molecular Weight:
301.25
Beilstein:
92214
EC Number:
MDL number:
UNSPSC Code:
12352204
PubChem Substance ID:
NACRES:
NA.32

product name

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

Assay

≥99% (TLC)

form

powder

solubility

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

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-IIRVCBMXSA-N

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Application

4-Nitrophenyl α-D-galactopyranoside has been used as a substrate to determine α-galactosidase activity.

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

Certificates of Analysis (COA)

Search for Certificates of Analysis (COA) by entering the products Lot/Batch Number. Lot and Batch Numbers can be found on a product’s label following the words ‘Lot’ or ‘Batch’.

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Effects of temperature and relative humidity on growth and enzyme production by Actinomucor elegans and Rhizopus oligosporus during sufu pehtze preparation
Han BZ, et al.
Food Chemistry, 81(1), 27-34 (2003)
Softwood hemicellulose-degrading enzymes from Aspergillus niger: purification and properties of a beta-mannanase
Ademark P, et al.
Journal of Biotechnology, 63(3), 199-210 (1998)
In vitro evaluation of feed-grade enzyme activity at pH levels simulating various parts of the avian digestive tract
Ao T, et al.
Anim. Feed Sci. Technol., 140(3-4), 462-468 (2008)
An acetylglucomannan esterase of Aspergillus oryzae; purification, characterization and role in the hydrolysis of O-acetyl-galactoglucomannan
Tenkanen M, et al.
Journal of Biotechnology, 42(3), 197-206 (1995)
Dhananjay S Kulkarni et al.
Biotechnology and applied biochemistry, 45(Pt 2), 51-57 (2006-06-20)
Alpha-galactosidase from Aspergillus oryzae was immobilized on chitosan beads using glutaraldehyde as a cross-linking agent. The general properties of free and immobilized enzymes were determined. The optimum pH for the free and immobilized enzymes was 4.8 and 4.6 respectively. The

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