추천 제품
재조합
expressed in E. coli
Quality Level
결합
(Lipid-linked)
양식
solution
분자량
58.9 kDa
배송 상태
dry ice
저장 온도
−20°C
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애플리케이션
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.
단위 정의
One unit will hydrolyze 1 μmol of asialo-GM1 per min at 37 °C at pH 5.0.
물리적 형태
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
개인 보호 장비
Eyeshields, Gloves, multi-purpose combination respirator cartridge (US)
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
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
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
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
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