E9030
Endoglycoceramidase II from Rhodococcus sp.
aqueous solution
Synonym(s):
EGCase, ceramide glycanase, glycosyl-N-acetyl-sphingosine 1,1-β-D-glucanohydrolase, oligoglycosylglucosyl(1↔1)ceramide glycohydrolase, oligoglycosylglucosylceramide glycohydrolase
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About This Item
Recommended Products
recombinant
expressed in E. coli
Quality Level
conjugate
(Lipid-linked)
form
solution
mol wt
58.9 kDa
shipped in
dry ice
storage temp.
−20°C
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Application
Endoglycoceramidase II from Rhodococcus sp. has been used in a study to assess the differentiation of glycosphingolipid-derived glycan structural isomers by liquid chromatography and mass spectrometry. Endoglycoceramidase II from Rhodococcus sp. has also been used in a study to investigate structural and mechanistic analyses of endo-glycoceramidase II.
Unit Definition
One unit will hydrolyze 1 μmol of asialo-GM1 per min at 37 °C at pH 5.0.
Physical form
Solution in 20 mM sodium acetate buffer, pH 6.0, containing 0.2% BSA and 0.1% Lubrol PX.
Storage Class Code
10 - Combustible liquids
WGK
WGK 3
Flash Point(F)
Not applicable
Flash Point(C)
Not applicable
Personal Protective Equipment
dust mask type N95 (US), Eyeshields, Gloves
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Journal of biochemistry, 130(2), 263-268 (2001-08-02)
Endoglycoceramidase (EGCase: EC 3.2.1.123) is an enzyme capable of cleaving the glycosidic linkage between oligosaccharides and ceramides in various glycosphingolipids. We report here transglycosylation and reverse hydrolysis reactions of EGCase from the jellyfish Cynaea nozakii. Various alkyl-GM1 oligosaccharides (alkyl-II(3)NeuAcGgOse4) were
The Journal of biological chemistry, 284(15), 9713-9726 (2009-02-12)
F18-fimbriated Escherichia coli are associated with porcine postweaning diarrhea and edema disease. Adhesion of F18-fimbriated bacteria to the small intestine of susceptible pigs is mediated by the minor fimbrial subunit FedF. However, the target cell receptor for FedF has remained
The Journal of biological chemistry, 282(15), 11386-11396 (2007-01-25)
Enzymes capable of hydrolyzing the beta-glycosidic linkage between oligosaccharides and ceramides in various glycosphingolipids has been found in microorganisms and invertebrates and designated endoglycoceramidase (EC 3.2.1.123) or ceramide glycanase. Here we report the molecular cloning, characterization, and homology modeling of
International journal for parasitology, 32(6), 677-684 (2002-06-14)
Glycolipids are important components of cellular membranes involved in various biological functions. In this report, we describe the identification of the de novo synthesis of glycosphingolipids by Toxoplasma gondii tachyzoites. Parasite-specific glycolipids were identified by metabolic labelling of parasites with
The Journal of biological chemistry, 282(19), 14300-14308 (2007-03-03)
endo-Glycoceramidase, a membrane-associated family 5 glycosidase, deviates from the typical polysaccharide substrate specificity of other soluble members of the family, preferentially hydrolyzing glycosidic linkages between the oligosaccharide and ceramide moieties of gangliosides. Here we report the first x-ray crystal structures
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