Described herein are methods of preparing a hypersialylated human immunoglobulin G (hsIgG) preparations.

A bender includes a rotatable bending shoe having at least one channel therein configured to receive a workpiece, a seat proximate to the bending shoe which is configured to receive the workpiece thereon, and a sensor provided on the seat which is configured to sense the presence of the workpiece. In some embodiments, the sensor is configured to sense an end of the workpiece.

The invention relates to a method of increasing the number of α2,3,-α2,6-disialylgalactose N-glycans on a glycoprotein by incubating an α2,3-sialylated glycoprotein with an α2,6-sialyltransferase and a sialic acid source. Also provided is a recombinant glycoprotein comprising at least one α2,3,-α2,6-disialylgalactose N-glycan. In a particular embodiment, the recombinant glycoprotein is alpha-1 antitrypsin (AAT).

Methods for making modified Fc regions of antibodies and antibody fragments, both human and humanized, and having enhanced stability and efficacy, are provided. Antibodies comprising Fc regions with core fucose residues removed, and attached to oligosaccharides comprising terminal sialyl residues, are provided. Antibodies comprising homogeneous glycosylation of Fc regions with specific oligosaccharides are provided. Fc regions conjugated with homogeneous glycoforms of monosaccharides and trisaccharides, are provided. Methods of preparing human antibodies with modified Fc using glycan engineering, are provided.

The present application relates to the field of glyco-engineering and, more specifically, to eukaryotic cells wherein both an endoglucosaminidase is present and made deficient in UDP-galactose 4-epimerase (GalE). Typically, a glycoprotein is also present in the cells. These cells can be used to deglycosylate or partly deglycosylate the (exogenous) glycoprotein, in particular, without the need for adding an extra enzyme. Methods are also provided for the application of these cells in protein production.

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

The present invention relates to the finding of methods to shift the glycosylation profile of recombinant produced semm glycoproteins to the predominant bi-antennary form found in human plasma. This is accomplished by providing a mammalian cell line according to the invention with a series of gene disruptions and/or gene insertions that facilitate this shift.

The present disclosure is directed to the properties of certain glycosyltransferase variants having N-terminal truncation deletions or internal deletions. Any of the mutants disclosed in here exhibit alpha-2,6-sialyltransferase enzymatic activity in the presence of CMP-activated sialic acid as co-substrate, and in the presence of a suitable acceptor site. A fundamental finding documented in the present disclosure is that these enzymes are not only capable of catalyzing transfer of a sialidyl moiety but they are also capable of catalyzing hydrolytic cleavage of terminally bound sialic acid from a glycan.

Disclosed herein are methods of generating proteoglycans with distinct glycan structures in engineered, non-naturally occurring eukaryotic cells. These methods make accessible a dynamic range of protein glycosylation. Compositions of engineered, non-naturally occurring cells capable of generating these proteoglycans are also disclosed herein.

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