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324716

Sigma-Aldrich

Endo-α-N-acetylgalactosaminidase, Streptococcus pneumoniae, Recombinant, E. coli

Endo-α-N-acetylgalactosaminidase, Streptococcus pneumoniae, Recombinant, E. coli, CAS 59793-96-3, catalyzes the hydrolysis of the unsubstituted Galβ1,3GalNAc core disaccharide attached to Ser or Thr.

Synonyme(s) :

Endo-α-N-acetylgalactosaminidase, Streptococcus pneumoniae, Recombinant, E. coli, O-Glycopeptide endo-D-galactosyl-N-acetyl-α-galactosaminohydrolase, O-Glycosidase

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About This Item

Numéro CAS:
59793-96-3
Numéro de classification (Commission des enzymes):
3.2.1.97 (BRENDA, IUBMB)
Code UNSPSC :
12352202
Nomenclature NACRES :
NA.42

Produit recombinant

expressed in E. coli

Niveau de qualité

100

Conjugué

(O-linked)

Forme

liquid

Activité spécifique

≥1 units/mL
≥10 units/mg protein

Fabricant/nom de marque

Calbiochem®

Conditions de stockage

do not freeze

Activité étrangère

N-acetylglucosaminidase, α- and β-galactosidase, α-mannosidase, neuraminidase, proteases, none detected

Conditions d'expédition

wet ice

Température de stockage

2-8°C

Catégories apparentées

Description générale

Note: 1 mU = 1 milliunit.
Recombinant, Streptococcus pneumoniae Endo-α-N-acetylgalactosaminidase expressed in E. coli. Catalyzes the hydrolysis of the unsubstituted Galβ1,3GalNAc core disaccharide attached to serine or threonine residues of glycopeptides and glycoproteins to afford free oligosaccharides.
Recombinant, Streptococcus pneumoniae Endo-α-N-acetylgalactosaminidase expressed in E. coli. Catalyzes the hydrolysis of the unsubstituted Galβ1,3GalNAc core disaccharide attached to serine or threonine residues of glycopeptides and glycoproteins to afford free oligosaccharides. For carbohydrates containing sialic acid or fucose, pretreatment with neuraminidase or fucosidase is required.

Avertissement

Toxicity: Standard Handling (A)

Définition de l'unité

One unit is defined as the amount of enzyme that will catalyze the release of 1.0 µmol p-nitrophenol from p-nitrophenyl-2-acetamido-2-deoxy-3-O-(β-D-galactopyranosyl)-α-D-galactopyranoside per min at 37°C, pH 5.0.

Forme physique

In 50 mM sodium phosphate buffer, pH 7.5.

Autres remarques

Wang, A.M., et al. 1998. Mol. Genet. Metab. 65, 165.
Iwase, H., and Hotta, K. 1993. Methods Mol. Biol. 14, 151.
Fan, J.Q., et al. 1990. Agric. Biol. Chem. 54, 233.
Umemoto, J., et al. 1978. Anal. Biochem. 91, 186.
Glasgow, L.R., et al. 1977. J. Biol. Chem. 252, 8615.

Informations légales

CALBIOCHEM is a registered trademark of Merck KGaA, Darmstadt, Germany

Code de la classe de stockage

10 - Combustible liquids

Classe de danger pour l'eau (WGK)

nwg

Point d'éclair (°F)

Not applicable

Point d'éclair (°C)

Not applicable

Certificats d'analyse (COA)

Recherchez un Certificats d'analyse (COA) en saisissant le numéro de lot du produit. Les numéros de lot figurent sur l'étiquette du produit après les mots "Lot" ou "Batch".

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Consulter la Bibliothèque de documents

Induction and efficient purification of endo-alpha-N-acetylgalactosaminidase from Alcaligenes sp.
J Q Fan et al.
Agricultural and biological chemistry, 54(1), 233-234 (1990-01-01)
J Umemoto et al.
Analytical biochemistry, 91(1), 186-193 (1978-11-01)
The synthetic glycosides, p-nitrophenyl- and o-nitrophenyl-2-acetamido-2-deoxy-3-O-beta-D-galactopyranosyl-alpha- D-galactopyranosides, were found to be effective chromogenic substrates for an endo-alpha-N-acetyl-D-galactosaminidase. We did not experience any problems when these substrates were used for the screening of column fractions during the purification of the endoenzyme
Release of O-linked glycoprotein glycans by endo-alpha-N-acetylgalactosaminidase.
H Iwase et al.
Methods in molecular biology (Clifton, N.J.), 14, 151-159 (1993-01-01)
Systematic purification of five glycosidases from Streptococcus (Diplococcus) pneumoniae.
L R Glasgow et al.
The Journal of biological chemistry, 252(23), 8615-8623 (1977-12-10)
A M Wang et al.
Molecular genetics and metabolism, 65(2), 165-173 (1998-10-27)
Recent characterization of the human sequences encoding two lysosomal hydrolases, alpha-galactosidase A (alpha-Gal A) and alpha-N-acetylgalactosaminidase (alpha-GalNAc) revealed that these two enzymes with distinct enzymatic activities shared about 50% overall amino acid identity and that their genomic sequences had a

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