Abstract: 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.

Abstract: The present invention provides methods of evaluating a glycoprotein preparation for the absence, presence or amount of an N-acetylhexosamine glycan, e.g., an N-acetylglucosamine glycan.

Abstract: Modified glycoproteins, and methods of making and using such modified glycoproteins, are described.

Abstract: Preparations of glycoproteins, e.g., therapeutic preparations of glycoproteins, having altered levels of affinity for Fc? receptors relative to reference glycoprotein preparations, and methods of making and methods of using such preparations, are described.

Abstract: The present invention relates to the characterization and production of denosumab.

Abstract: Among other things, the present disclosure provides methods for enriching, identifying, and/or quantifying unusually modified glycans (e.g., phosphorylated glycans, sulfated glycans, and/or multi-acetylated glycans). In many embodiments, methods comprise providing a glycan preparation from which sialic acids have been released; subjecting the sialidase-treated glycan preparation to a separation technique that separates glycans based on charge-to-mass ratio; and quantifying the charged products using at least one quantification standard.

Abstract: Glycoproteins having particular sialylation patterns, and methods of making and using such glycoproteins, are described.

Abstract: Methods of making and evaluating antibody biological therapeutics (biosimilars) for adalimumab, rituximab and panitumumab are disclosed.

Abstract: Production and bioanalytical characterization of determinative parameters of adalimumab is presented.

Abstract: The present invention relates to the characterization and production of panitumumab.

Abstract: The present invention relates to the characterization and production of bevacizumab.

Abstract: The present invention relates to the characterization and production of rituximab.

Abstract: The present invention relates to the characterization and production of omalizumab.

Abstract: 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.

Abstract: The present invention relates to the characterization and production of alemtuzumab.

Abstract: The present invention relates to the characterization and production of trastuzumab. The present disclosure provides, in part, methods for evaluating, identifying, and/or producing (e.g., manufacturing) trastuzumab. In some instances, methods herein allow highly resolved evaluation of trastuzumab useful for, inter alia, manufacturing trastuzumab, characterizing trastuzumab, identifying and/or confirming trastuzumab, monitoring the structure of trastuzumab, comparing trastuzumab preparations made over time or made under different conditions, and/or controlling the structure of trastuzumab.

Abstract: 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.

Abstract: Sulfated glycoproteins, and methods of making and using such sulfated glycoproteins, are described.

Abstract: 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.

Abstract: 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.