| 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 |
| 20100133430 | MS METHODS TO EVALUATE GLYCANS - The present disclosure provides, among other things, methods for the identification of sulfated glycans in a mixture of glycans. | 06-03-2010 |
| 20100151499 | PROTEOLYTIC RELEASE OF GLYCANS - The present disclosure provides strategies for analyzing protein-linked glycans, and particularly for analyzing glycans on cell surface glycoproteins. | 06-17-2010 |
| 20100151584 | MULTI-DIMENSIONAL CHROMATOGRAPHIC METHODS FOR SEPARATING N-GLYCANS - A multi-dimensional chromatographic method for the separation of N-glycans. The method comprises providing a glycan preparation that includes at least one negatively charged N-glycan. The glycan preparation is then separated by anion-exchange chromatography and at least one secondary chromatographic technique. | 06-17-2010 |
| 20100188084 | COMPARATIVE ANALYSIS OF PROTEIN CONFORMATIONS BY USING 2D NOESY NMR SPECTRA - The present disclosure provides a method for determining the relative conformations of a protein provided in different protein preparations, comprising steps of: (i) obtaining a first 2D NOESY NMR spectrum of a first protein preparation; (ii) obtaining a second 2D NOESY NMR spectrum of a second protein preparation; and (iii); determining whether a protein has a different conformation in the first and second protein preparations by comparing one or more cross-peaks in the first 2D NOESY NMR spectrum with one or more corresponding cross-peaks in the second 2D NOESY NMR spectrum. | 07-29-2010 |
| 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 |
| 20100279269 | CHARACTERIZATION OF N-GLYCAN MIXTURES BY NUCLEAR MAGNETIC RESONANCE - The present disclosure provides nuclear magnetic resonance (NMR) methods for characterizing mixtures of N-linked glycans. Without limitation, methods of the present disclosure may be useful in characterizing monosaccharide composition, branching, fucosylation, sulfation, phosphorylation, sialylation linkages, presence of impurities and/or efficiency of a labeling procedure (e.g., labeling with a fluorophore such as 2-AB). In certain embodiments, the methods can be used quantitatively. In certain embodiments, the methods can be combined with enzymatic digestion to further characterize glycan mixtures. | 11-04-2010 |
| 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 |
| 20110136682 | ANTENNARY FUCOSYLATION IN GLYCOPROTEINS FROM CHO CELLS - The present invention provides methods of evaluating CHO cells and producing recombinant glycoproteins. | 06-09-2011 |
