E6878
Endoglycosidase H from Streptomyces griseus
lyophilized powder
Synonym(s):
β-N-Acetylglucosaminidase H
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About This Item
form
lyophilized powder
shipped in
dry ice
storage temp.
−20°C
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Unit Definition
One unit will hydrolyze 1.0 μmole of N-acetyl-(14C)Asn(GlcNAc)2(Man)5 per min at pH 5.0 at 37 °C.
Physical form
Lyophilized powder containing bovine serum albumin
signalword
Danger
hcodes
pcodes
Hazard Classifications
Resp. Sens. 1
Storage Class
10 - Combustible liquids
wgk_germany
WGK 1
flash_point_f
Not applicable
flash_point_c
Not applicable
ppe
Eyeshields, Gloves, multi-purpose combination respirator cartridge (US)
Certificates of Analysis (COA)
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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
PloS one, 6(8), e23838-e23838 (2011-08-23)
Hepatitis C Virus E1E2 heterodimers are components of the viral spike. Although there is a general agreement on the necessity of the co-expression of both E1 and E2 on a single coding unit for their productive folding and assembly, in
Carbohydrate research, 345(17), 2458-2463 (2010-10-12)
To determine the structural specificity of the glycosyl acceptor of the transglycosylation reaction using endo-β-N-acetylglucosaminidase (ENGase) (EC 3.2.1.96) from Mucor hiemalis (Endo-M), several acceptor derivatives were designed and synthesized. The narrow regions of the 1,3-diol structure from the 4- to
Prikladnaia biokhimiia i mikrobiologiia, 46(4), 448-455 (2010-09-29)
The HuIFNA16, HuIFNB, and BoIFNG genes encoding human [alpha]16, beta-interferons and bovine gamma-interferon were cloned under the control of the yeast Pichia pastoris AOX1 gene promoter. The yeast strains producing heterologous interferons intracellularly and extracellularly were constructed. There was no
Aging, 3(10), 968-984 (2011-10-13)
A distinct conformational transition from the α-helix-rich cellular prion protein (PrPC) into its β-sheet-rich pathological isoform (PrPSc) is the hallmark of prion diseases, a group of fatal transmissible encephalopathies that includes spontaneous and acquired forms. Recently, a PrPSc-like intermediate form
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