产品名称
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.
recombinant
expressed in E. coli
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
Quality Level
Disclaimer
Toxicity: Standard Handling (A)
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. For carbohydrates containing sialic acid or fucose, pretreatment with neuraminidase or fucosidase is required.
Other Notes
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.
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.
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.
Physical form
In 50 mM sodium phosphate buffer, pH 7.5.
Legal Information
CALBIOCHEM is a registered trademark of Merck KGaA, Darmstadt, Germany
存储类别
10 - Combustible liquids
wgk
nwg
flash_point_f
Not applicable
flash_point_c
Not applicable
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)
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
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
商品
Learn about O-linked glycan strategies, O-glycosidase actions, how to remove sialic acid residues, β-Elimination, and O-glycan modifications.
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