glyco application

Recombinant Glycoprotein Expression

Recombinant expression of glycoproteins is of great interest, particularly in the production of therapeutic glycoproteins such as immunoglobulins and hormones for the biopharmaceutical market. Each expression system has its advantages and disadvantages (1).  Some factors to be aware of when choosing an expression system are:

  • Bacterial systems cannot produce a protein with mammalian-type glycosylation.
  • Yeast primarily modifies glycoproteins with only high mannose N-glycans.
  • Plant and insect cell lines can modify N-glycans with a core α1-3 fucose residue not found in humans.
  • Plants can also add a non-human xylose residue to the N-glycan.
  • Some mammalian cell lines can add the non-human epitopes Gal α1-3 Gal or N-glycolylneuraminic acid (NGNA) to glycoproteins.


  1. Betenbaugh M.J., et al (2004) Curr Opin Struct Biol. 14(5):601-6. PMID: 15465322

Choose Type:

Recombinant Glycoprotein Expression includes these areas of focus:
Expression Systems
FAQs for Recombinant Glycoprotein Expression
Protocols for Recombinant Glycoprotein Expression
Legal Information

Products and content are covered by one or more patents, trademarks and/or copyrights owned or controlled by New England Biolabs, Inc (NEB). The use of trademark symbols does not necessarily indicate that the name is trademarked in the country where it is being read; it indicates where the content was originally developed. The use of this product may require the buyer to obtain additional third-party intellectual property rights for certain applications. For more information, please email

This product is intended for research purposes only. This product is not intended to be used for therapeutic or diagnostic purposes in humans or animals.