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Key Documents

A0810

Sigma-Aldrich

Endoglycosidase H from Streptomyces plicatus

recombinant, expressed in E. coli, buffered aqueous solution

Synonym(s):

β-N-Acetylglucosaminidase H

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About This Item

CAS Number:
Enzyme Commission number:
MDL number:
UNSPSC Code:
12352204
NACRES:
NA.32

recombinant

expressed in E. coli

Quality Level

conjugate

(N-linked)

form

buffered aqueous solution

shipped in

wet ice

storage temp.

2-8°C

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General description

Endoglycosidase H or endo-β-N-acetylglucosaminidase H is an glycohydrolase. It is produced by Streptomyces plicatus and other Streptomyces species.

Biochem/physiol Actions

Endoglycosidase H is involved in cleaving the N-linked glycans present between the two N-acetylglucosamine (GlcNAc) residues in the core of the glycan chain in high-mannose sugars.

Unit Definition

One unit will release N-linked oligosaccharides from 1 μmole of denatured ribonuclease B per min at 37 °C at pH 5.5.

Physical form

Solution in 20 mM Tris HCl, pH 7.5, containing 50 mM NaCl, 1 mM EDTA

Storage Class Code

12 - Non Combustible Liquids

WGK

WGK 1

Flash Point(F)

Not applicable

Flash Point(C)

Not applicable

Personal Protective Equipment

dust mask type N95 (US), Eyeshields, Gloves

Certificates of Analysis (COA)

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High-Level Expression of Endo-
Freeze H H and Kranz C
Current Protocols in Molecular Biology, 0 17(3) (2010)
High-Level Expression of Endo-
Wang F, et al.
Testing, 10(3) (2015)
Ingeborg Stals et al.
PloS one, 7(7), e40854-e40854 (2012-08-04)
Endo-N-acetyl-β-D-glucosaminidases (ENGases) hydrolyze the glycosidic linkage between the two N-acetylglucosamine units that make up the chitobiose core of N-glycans. The endo-N-acetyl-β-D-glucosaminidases classified into glycoside hydrolase family 18 are small, bacterial proteins with different substrate specificities. Recently two eukaryotic family 18
Wei Zhang et al.
Talanta, 85(1), 499-505 (2011-06-08)
Endoglycosidase is a class of glycosidases that specifically cleaves the glycosidic bond between two proximal residues of GlcNAc in the pentasaccharide core of N-glycan, leaving the innermost GlcNAc still attached to its parent protein, which provides a different diagnostic maker
Ulla-Maja Bailey et al.
Journal of chromatography. B, Analytical technologies in the biomedical and life sciences, 923-924, 16-21 (2013-03-05)
Post-translational modification of proteins with glycosylation is of key importance in many biological systems in eukaryotes, influencing fundamental biological processes and regulating protein function. Changes in glycosylation are therefore of interest in understanding these processes and are also useful as

Articles

Explore strategies for releasing N-linked glycans with PNGase F, PNGase A & native & sequential deglycosylation with endoglycosidases & exoglycosidases.

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