Patent application number | Description | Published |
20100129843 | CHARACTERIZATION OF N-GLYCANS USING EXOGLYCOSIDASES - The present disclosure provides methods for analyzing structure and/or composition of N-glycans. Such methods often involve digestion of N-glycans with multiple exoglycosidases. In some embodiments, N-glycans are digested with multiple exoglycosidases simultaneously. In some embodiments, N-glycans are digested with multiple exoglycosidases sequentially. In some embodiments, methods in accordance with the present disclosure involve comparison of cleavage products of N-glycans that have been digested with multiple exoglycosidases simultaneously to N-glycans that have been digested with multiple exoglycosidases sequentially. | 05-27-2010 |
20100196940 | METHODS RELATED TO CELL SURFACE GLYCOSYLATION - The present disclosure provides methods for assessing the glycosylation of a target glycoprotein produced by a cell through analysis of cell-surface glycans on the cell. The present disclosure therefore teaches that glycosylation of cell surface proteins can serve as a proxy for glycosylation of other proteins. | 08-05-2010 |
20100279306 | ANALYSIS OF PHOSPHORYLATED GLYCANS, GLYCOPEPTIDES OR GLYCOPROTEINS BY IMAC - The present disclosure provides technologies for enriching, detecting, and/or quantifying phosphorylated glycans and/or glycoconjugates (e.g., glycopeptides, glycolipids, proteoglycans, etc.). Specifically, the present disclosure provides methods that utilize immobilized metal affinity chromatography (IMAC) to isolate and/or to characterize phosphorylated glycans. The present disclosure particularly provides methods for distinguishing sulfated and phosphorylated glycans. | 11-04-2010 |
20110213137 | ISOTOPICALLY-LABELED GLYCANS - The present disclosure provides methods of making isotopically-labeled glycans or a mixture of glycans (e.g., a glycan preparation) via reductive amination. Such methods are useful, for example, in the determination of the relative amounts of a glycan species present in two or more glycoprotein preparations using mass spectroscopy. In one aspect, the present disclosure provides a method of making an isotopically-labeled glycan by a glycan with an amine and an isotopically-labeled reducing agent to provide an isotopically-labeled aminated glycan. In certain embodiments, the amine is an isotopically-labeled amine. | 09-01-2011 |
20120264927 | METHODS FOR LABELING GLYCANS - Methods for labeling glycans that include a step of freeze-drying a labeled glycan preparation. The labeled glycan preparation is maintained in a substantially frozen state for the duration of the freeze-drying process. | 10-18-2012 |
20120277165 | METHODS OF MODULATING FUCOSYLATION OF GLYCOPROTEINS - The present invention provides methods and materials useful for monitoring and regulating the glycosylation of glycoproteins that are recombinantly produced from cells. In particular, methods are provided for monitoring and regulating levels of cellular indicators which affect the level of fucosylation produced by cells. | 11-01-2012 |
20120329709 | PRODUCTION OF GLYCOPROTEINS - The present invention provides methods and materials by which glycosylation of glycoproteins can be regulated. Methods include the monitoring and regulation of parameters such that a glycoprotein having a desired product quality is obtained. | 12-27-2012 |
20130123126 | SELECTION AND USE OF HOST CELLS FOR PRODUCTION OF GLYCOPROTEINS - A method of making a glycoprotein having a selected glycostructure. | 05-16-2013 |
20130184180 | CHARACTERIZATION OF N-GLYCANS USING EXOGLYCOSIDASES - The present disclosure provides methods for analyzing structure and/or composition of N-glycans. Such methods often involve digestion of N-glycans with multiple exoglycosidases. In some embodiments, N-glycans are digested with multiple exoglycosidases simultaneously. In some embodiments, N-glycans are digested with multiple exoglycosidases sequentially. In some embodiments, methods in accordance with the present disclosure involve comparison of cleavage products of N-glycans that have been digested with multiple exoglycosidases simultaneously to N-glycans that have been digested with multiple exoglycosidases sequentially. | 07-18-2013 |