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.

References:

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

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