E9030
Endoglycoceramidase II from Rhodococcus sp.
aqueous solution
别名:
EGCase, ceramide glycanase, glycosyl-N-acetyl-sphingosine 1,1-β-D-glucanohydrolase, oligoglycosylglucosyl(1↔1)ceramide glycohydrolase, oligoglycosylglucosylceramide glycohydrolase
产品名称
Endoglycoceramidase II from Rhodococcus sp., aqueous solution
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
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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.
Other Notes
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.
存储类别
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)
法规信息
新产品
此项目有
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
Kentaro Tsukamoto et al.
The Journal of biological chemistry, 280(42), 35164-35171 (2005-08-24)
Clostridium botulinum neurotoxins (BoNTs) act on nerve endings to block acetylcholine release. Their potency is due to their enzymatic activity and selective high affinity binding to neurons. Although there are many pieces of data available on the receptor for BoNT
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
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
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