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Key Documents

N4264

Sigma-Aldrich

4-Nitrophenyl N-acetyl-α-D-galactosaminide

galactosaminide substrate, ≥98% (TLC), powder

Synonyma:

p-Nitrophenyl 2-acetamido-2-deoxy-α-D-galactopyranoside

Přihlásitk zobrazení cen stanovených pro organizaci a smluvních cen


About This Item

Empirický vzorec (Hillův zápis):
C14H18N2O8
Číslo CAS:
Molekulová hmotnost:
342.30
EC Number:
MDL number:
UNSPSC Code:
12352204
PubChem Substance ID:
NACRES:
NA.32

product name

4-Nitrophenyl N-acetyl-α-D-galactosaminide, substrate for N-acetyl-α-D-galactosaminidase

assay

≥98% (TLC)

form

powder

solubility

DMF: 25 mg/mL, clear, colorless to faintly yellow

storage temp.

−20°C

SMILES string

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

InChI

1S/C14H18N2O8/c1-7(18)15-11-13(20)12(19)10(6-17)24-14(11)23-9-4-2-8(3-5-9)16(21)22/h2-5,10-14,17,19-20H,6H2,1H3,(H,15,18)/t10-,11-,12+,13-,14+/m1/s1

InChI key

OMRLTNCLYHKQCK-RGDJUOJXSA-N

Biochem/physiol Actions

4-Nitrophenyl N-acetyl-α-D-galactosaminide serves as a chromogenic synthetic substrate for lysosomal enzyme α-N-acetylgalactosaminidase to perform enzyme assays. Upon cleavage the substrate forms a yellow color solution of p-nitrophenol that can be measured at 400nm at pH 10.6.

Storage Class

11 - Combustible Solids

wgk_germany

WGK 3

flash_point_f

Not applicable

flash_point_c

Not applicable


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Simon P J Albracht et al.
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This paper presents a new assay to determine the activity of the lysosomal enzyme α-N-acetylgalactosaminidase (Naga, EC 3.2.1.49) in human serum. It is based on the use of a new chromogenic substrate, DNP-α-GalNAc (2,4-dinitrophenyl-N-acetyl-α-D-galactosaminide) and is performed at pH 4.3 and
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Jin-Jin Xie et al.
Journal of biomolecular structure & dynamics, 26(4), 509-515 (2008-12-26)
Beta-N-acetyl-D-glucosaminidase (NAGase, EC.3.2.1.52), which catalyzes the cleavage of N-acetylglucosamine polymers, is a composition of chitinase and cooperates with endo-chitinase and exo-chitinase to disintegrate chitin into N-acetylglucosamine (NAG). In this investigation, A NAGase from green crab (Scylla serrata) was purified and
R D Roer et al.
Comparative biochemistry and physiology. Part B, Biochemistry & molecular biology, 128(4), 683-690 (2001-04-06)
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