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E9030

Sigma-Aldrich

Endoglycoceramidase II from Rhodococcus sp.

aqueous solution

Synonim(y):

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

Numer EC enzymu:
3.2.1.123 (BRENDA, IUBMB)
Numer MDL:
MFCD03456712
Kod UNSPSC:
12352204
NACRES:
NA.54

rekombinowane

expressed in E. coli

Poziom jakości

200

białko sprzężone

(Lipid-linked)

Postać

solution

masa cząsteczkowa

58.9 kDa

Warunki transportu

dry ice

temp. przechowywania

−20°C

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Zastosowanie

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.

Definicja jednostki

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

Postać fizyczna

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

10 - Combustible liquids

Klasa zagrożenia wodnego (WGK)

WGK 3

Temperatura zapłonu (°F)

Not applicable

Temperatura zapłonu (°C)

Not applicable

Środki ochrony indywidualnej

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

Certyfikaty analizy (CoA)

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Dokumenty związane z niedawno zakupionymi produktami zostały zamieszczone w Bibliotece dokumentów.

Odwiedź Bibliotekę dokumentów

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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