Glycoengineering of Proteins

In vitro glycosylation of proteins is an important technology for pharmaceutical development. The targeted modification of therapeutic antibodies allows attenuation of active profiles. Key components are glycosyltransferases and the activated sugars.

Custom Biotech offers the most relevant sugar moieties and glycosyltransferases to build typical mammalian glycan structures. Current development efforts are focusing on the availability of further glycosyltransferases. Enzymes and activated sugars are produced recombinantly and are free of any animal-derived components. They are available as non-GMP products for analytical and R&D purposes but also as GMP grades upon request.


Glycosylation of Proteins

Custom Biotech provides activated sugars and related transferase enzymes for in vitro modification of glycan structures and transfer of sugar moieties. 

For in vitro galctosylation of GlcNAc1-2Man units on glycoproteins, use ß-1,4-Galactosyltransferase and UDP-Galactose. In vitro sialylation of al Galß1-4GlcNAc units on glycoproteins can be achieved using a 2,6-Sialyltransferase and CMP-NANA.


Deglycosylation of Proteins

Roche also provides several enzymes for deglycosylation. Choose N-Glycosidase F to cleave all types of asparagine-bound N-glycans, or N-Glycosidase A (PNGase A) to remove single N-acetyl-glucosamine residuals and also N-bound glycans, including high mannose-, hybrid-, tri-, and tetraantennary complexes. For removal of N- and O-acetylneuraminic acids Custom Biotech offers Neuraminidase (exo-α-sialidase).