Glycoengineering of Proteins
In vitro glycosylation of proteins is a novel technology to develop and manufacture next-generation biopharmaceuticals by directed modification of the glycosylation of therapeutic proteins.
Control and management of the glycosylation pattern of therapeutic proteins, such as recombinant monoclonal antibodies, plays an important role in the biopharmaceutical industry. It is well known that pharmacodynamics and pharmacokinetic properties of a biopharmaceutical can be highly improved by optimization of its glycosylation pattern.
Custom Biotech has developed highly active glycosyltransferases to add galactosyl- and sialyl-residues to glycan chains of glycoproteins. Together with the corresponding activated sugars and glycosidases a set of tools is provided that enables our customers to engineer the glycosylation pattern of therapeutic proteins, e.g. increasing homogeneity of the glycopattern.
Glycosylation of Proteins
Human β-1,4-Galactosyltransferase and α-2,6-Sialyltransferase catalyze the addition of galactosyl- and sialyl-residues to glycans. Custom Biotech provides both recombinant enzymes to the biopharma industry, produced completely free of animal components and available in GMP grade upon request. The corresponding activated sugars UDP-Galactose and CMP-NANA required as donor-substrates are also available.
Deglycosylation of Proteins
Roche also provides enzymes for deglycosylation: Neuraminidase and β-Galactosidase can be used in the process of re-engineering the glycan structure of therapeutic proteins to remove sialyl- and galactosyl-residues from glycans.
N-Glycosidase F (PNGase F) is used to cleave N-glycans from Glycoproteins for analytic purposes.