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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

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
T Tai et al.
The Journal of biological chemistry, 250(21), 8569-8575 (1975-11-10)
Heterogeneities of the two ovalbumin glycopeptides, (Man)5(GlcNAc)2Asn and (Man)6(GlcNAc)2Asn, were revealed by borate paper electrophoresis of oligosaccharide alcohols obtained from the glycopeptides by endo-beta-N-acetylglucosaminidase H digestion and NaB3H4 reduction. The structures of the major components of the oligosaccharides were determined

Articles

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

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