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Merck
CN

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

UNSPSC Code:
12352204
NACRES:
NA.54
EC Number:
3.2.1.123 (BRENDA, IUBMB)
MDL number:
MFCD03456712
Recombinant:
expressed in E. coli

Key Documents

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recombinant

expressed in E. coli

conjugate

(Lipid-linked)

form

solution

mol wt

58.9 kDa

shipped in

dry ice

storage temp.

−20°C

Quality Level

200

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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.

Physical form

Solution in 20 mM sodium acetate buffer, pH 6.0, containing 0.2% BSA and 0.1% Lubrol PX.

Other Notes

One unit will hydrolyze 1 μmol of asialo-GM1 per min at 37 °C at pH 5.0.

Storage Class

10 - Combustible liquids

wgk

WGK 3

flash_point_f

Not applicable

flash_point_c

Not applicable

ppe

Eyeshields, Gloves, multi-purpose combination respirator cartridge (US)

Regulatory Information

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Certificates of Analysis (COA)

Lot/Batch Number
SLCM6490
SLCM6489
SLCL8894
SLCF1643
SLCC3534

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Yohei Ishibashi et al.
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
Y Horibata et al.
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
Annelies Coddens et al.
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
Hasse Karlsson et al.
Glycobiology, 20(9), 1103-1116 (2010-05-15)
Isolation and characterization of glycosphingolipids is of importance in many aspects of glycobiology, but is difficult to achieve due to the high degree of heterogeneity and isomerism present in these compounds. In this study, oligosaccharides obtained from non-acid glycosphingolipids by
Yohei Ishibashi et al.
Journal of biochemistry, 142(2), 239-246 (2007-06-15)
Endoglycoceramidase is a glycohydrolase capable of hydrolysing the O-glycosidic linkage between oligosaccharides and ceramides of various glycosphingolipids. However, no endoglycoceramidase reported so far can hydrolyse 6-gala series glycosphingolipids which possess the common structure R-Gal beta1-6Gal beta1-1'Cer. Recently, we found a
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