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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.

别名:

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号:
59793-96-3
EC 号:
3.2.1.97 (BRENDA, IUBMB)
分類程式碼代碼:
12352202
NACRES:
NA.42

重組細胞

expressed in E. coli

品質等級

100

共軛

(O-linked)

形狀

liquid

比活性

≥1 units/mL
≥10 units/mg protein

製造商／商標名

Calbiochem®

儲存條件

do not freeze

異物活動

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

運輸包裝

wet ice

儲存溫度

2-8°C

相关类别

一般說明

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.

警告

Toxicity: Standard Handling (A)

單位定義

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.

外觀

In 50 mM sodium phosphate buffer, pH 7.5.

其他說明

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.

法律資訊

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

儲存類別代碼

10 - Combustible liquids

水污染物質分類（WGK）

nwg

閃點（°F）

Not applicable

閃點（°C）

Not applicable

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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)

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O-Linked Glycan Strategies

Learn about O-linked glycan strategies, O-glycosidase actions, how to remove sialic acid residues, β-Elimination, and O-glycan modifications.

O-Linked Glycan Strategies

Learn about O-linked glycan strategies, O-glycosidase actions, how to remove sialic acid residues, β-Elimination, and O-glycan modifications.

O-Linked Glycan Strategies

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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