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N4264

Sigma-Aldrich

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

galactosaminide substrate, ≥98% (TLC), powder

Synonym(e):

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

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About This Item

Empirische Formel (Hill-System):
C14H18N2O8
CAS-Nummer:
23646-68-6
Molekulargewicht:
342.30
EG-Nummer:
245-802-3
MDL-Nummer:
MFCD00065476
UNSPSC-Code:
12352204
PubChem Substanz-ID:
24897699
NACRES:
NA.32

product name

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

Assay

≥98% (TLC)

Form

powder

Löslichkeit

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

Lagertemp.

−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

InChIKey

OMRLTNCLYHKQCK-RGDJUOJXSA-N

Verwandte Kategorien

Biochem./physiol. Wirkung

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.

Lagerklassenschlüssel

11 - Combustible Solids

WGK

WGK 3

Flammpunkt (°F)

Not applicable

Flammpunkt (°C)

Not applicable

Analysenzertifikate (COA)

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N-Acetyl-D-galactosamin ≥98% (HPLC)

Sigma-Aldrich

A2795

N-Acetyl-D-galactosamin

4-Nitrophenyl β-D-Glucopyranosid ≥98% (TLC)

Sigma-Aldrich

N7006

4-Nitrophenyl β-D-Glucopyranosid

Simon P J Albracht et al.
BBA clinical, 8, 84-89 (2017-10-25)
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
Jeffrey B Kaplan et al.
Journal of bacteriology, 185(16), 4693-4698 (2003-08-05)
When cultured in broth, fresh clinical isolates of the gram-negative periodontal pathogen Actinobacillus actinomycetemcomitans form tenaciously adherent biofilm colonies on surfaces such as plastic and glass. These biofilm colonies release adherent cells into the medium, and the released cells can
O Habuchi et al.
The Journal of biological chemistry, 260(24), 13102-13108 (1985-10-25)
Chick embryo chondrocyte microsomes containing intact Golgi vesicles took up 3'-phosphoadenosine-5'-phospho[35S]sulfate ([35S]PAPS) in a time- and temperature-dependent, substrate-saturable manner. When [35S]PAPS and p-nitrophenyl-N-acetyl-beta-D-galactosaminide (pNP-GalNAc) were added to the incubation in the absence of detergent, the microsomes catalyzed the transfer of
S Singh et al.
Carbohydrate research, 305(3-4), 363-370 (1998-07-02)
The beta-N-acetylhexosaminidase from Aspergillus oryzae catalysed the transfer of beta-D-N-acetylgalactosaminyl residues from p-nitrophenyl beta-D-N-acetylglucosaminide on to disaccharide acceptors consisting of thioethyl glycosides of alpha-D-Glc-(1-->4)-beta-D-Glc, beta-D-Glc-(1-->4)-beta-D-Glc and beta-D-Glc-(1-->6)-beta-D-Glc. The principle of 'anomeric control' was exemplified by the results which showed that
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
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