Conduritol B Epoxide, Conduritol B Epoxide, CAS 6090-95-5, is an irreversible Inhibitor of glucocerebrosidase in neurons. Also inhibits α-glucosidase activity in a variety of species.
Inhibits α-glucosidase activity in mammals, snails, sweet almonds and yeast. An irreversible, potent, and specific inhibitor of glucocerebrosidase in cultured neurons. Has also been shown to inhibit α-glucosidase from yeast, and rabbit intestinal sucrase-isomaltase complex.
Inhibits α-glucosidase activity in mammals, snails, sweet almonds, and yeast. An irreversible, potent, and specific inhibitor of glucocerebrosidase in cultured neurons. Has also been shown to inhibit α-glucosidase from yeast and rabbit intestinal sucrase-isomaltase complex.
Biochem/physiol Actions
Cell permeable: no
Primary Target α-glucosidase
Product does not compete with ATP.
Reversible: no
Warning
Toxicity: Harmful (C)
Reconstitution
Unstable in solution; reconstitute just prior to use.
CALBIOCHEM is a registered trademark of Merck KGaA, Darmstadt, Germany
Storage Class
11 - Combustible Solids
wgk_germany
WGK 3
flash_point_f
Not applicable
flash_point_c
Not applicable
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Proceedings of the National Academy of Sciences of the United States of America, 117(44), 27646-27654 (2020-10-17)
Neurons are dependent on proper trafficking of lipids to neighboring glia for lipid exchange and disposal of potentially lipotoxic metabolites, producing distinct lipid distribution profiles among various cell types of the central nervous system. Little is known of the cellular
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Proceedings of the National Academy of Sciences of the United States of America, 118(31) (2021-07-31)
Loss-of-function mutations in acid beta-glucosidase 1 (GBA1) are among the strongest genetic risk factors for Lewy body disorders such as Parkinson's disease (PD) and Lewy body dementia (DLB). Altered lipid metabolism in PD patient-derived neurons, carrying either GBA1 or PD
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Homozygotic mutations in the GBA gene cause Gaucher's disease; moreover, both patients and heterozygotic carriers have been associated with 20- to 30-fold increased risk of developing Parkinson's disease. In homozygosis, these mutations impair the activity of β-glucocerebrosidase, the enzyme encoded
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