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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.

Synonym(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

CAS Number:
59793-96-3
Enzyme Commission number:
3.2.1.97 (BRENDA, IUBMB)
UNSPSC Code:
12352202
NACRES:
NA.42

recombinant

expressed in E. coli

Quality Level

100

conjugate

(O-linked)

form

liquid

specific activity

≥1 units/mL
≥10 units/mg protein

manufacturer/tradename

Calbiochem®

storage condition

do not freeze

foreign activity

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

shipped in

wet ice

storage temp.

2-8°C

Related Categories

General description

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.

Warning

Toxicity: Standard Handling (A)

Unit Definition

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.

Physical form

In 50 mM sodium phosphate buffer, pH 7.5.

Other Notes

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.

Legal Information

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

Storage Class

10 - Combustible liquids

wgk_germany

nwg

flash_point_f

Not applicable

flash_point_c

Not applicable

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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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)
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
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)

Articles

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