EC Number   |
Application |
Reference |
|---|
   3.2.1.123 | drug development |
rational redesign of EGC toward the synthesis of novel ganglioside-derived therapeutics |
680770 |
| 3.2.1.123 | medicine |
release of glycans from the ceramide moieties of glycosphingolipids by endoglycoceramidase II treatment in order to analyze structures of glycosphingolipids in normal human colorectal epithelial cells, and characteristic alterations of oligosaccharide structures in malignant transformation |
699823 |
| 3.2.1.123 | analysis |
the enzyme can be used for comprehensive profiling of glycosphingolipid glycans in a high-throughput workflow. The existing robotized N-glycan analysis platform is adapted for the quantitative high-throughput profiling of 2AB-fluorescent-labeled mammalian glycosphingolipid head groups using ultraperformance hydrophilic interaction liquid chromatography with fluorescence detection (UPLC-HILIC-FLD). An enabling component of the glycosphingolipid glycan workflow is the identification and characterization of the recombinant EGCase I enzyme from Rhodocococcus triatomea that exhibits a broad glycosphingolipid specificity, including the release of globo-series glycosphingolipids and Gal(beta1<->1)Cer, important classes of glycosphingolipids that are not efficiently released by known EGCases. The ability is demonstrated to characterize glycosphingolipid head groups from both mammalian cell surfaces and small volumes of blood serum. This analytical workflow will permit further exploration of the glycosphingolipid headgroup repertoire of glycosphingolipids from a broad range of biological sources and will enable studies aiming to identify cellular or serum glycosphingolipid-glycan biomarkers of disease |
-, 749565 |
| 3.2.1.123 | diagnostics |
the enzyme can be used for comprehensive profiling of glycosphingolipid glycans in a high-throughput workflow. The existing robotized N-glycan analysis platform is adapted for the quantitative high-throughput profiling of 2AB-fluorescent-labeled mammalian glycosphingolipid head groups using ultraperformance hydrophilic interaction liquid chromatography with fluorescence detection (UPLC-HILIC-FLD). An enabling component of the glycosphingolipid glycan workflow is the identification and characterization of the recombinant EGCase I enzyme from Rhodocococcus triatomea that exhibits a broad glycosphingolipid specificity, including the release of globo-series glycosphingolipids and Gal(beta1<->1)Cer, important classes of glycosphingolipids that are not efficiently released by known EGCases. The ability is demonstrated to characterize glycosphingolipid head groups from both mammalian cell surfaces and small volumes of blood serum. This analytical workflow will permit further exploration of the glycosphingolipid headgroup repertoire of glycosphingolipids from a broad range of biological sources and will enable studies aiming to identify cellular or serum glycosphingolipid-glycan biomarkers of disease |
-, 749565 |
