Protein Modification

Glycosylation is perhaps the most common and versatile post-translational modification of proteins. It is estimated that well over one-half of all mammalian proteins are glycosylated. The roles of protein glycans, whether N- or O-linked forms, are varied. Glycan is required for the biological function of certain proteins, such as,

  1. The Fc-effector function of immunoglobulin G (IgG).

  2. The regulated clearance of the glycohormone lutropin (LH),

  3. The targeting of lysosomal enzymes and,

  4. Controlling the circulation lifetime of glycoprotein drugs (for example,  erythropoietin)

Glycans can also serve as:

1. Recognition targets for their complementary binding proteins, the lectins.
2. Serving as sites of attachment by microbes and toxins, and often constitute the first contact point between pathogen and host.
3. Protecting proteins from proteolytic enzymes.
4. Promoting protein foldinginto proper tertiary and quaternary structure.
5. Modulating the biological activities of protein.
   

Interestingly, N-glycosylation pathway of baculovirus infected insect cells differs from the pathway found in higher eukaryotes, as indicated by the fact that glycoproteins produced in the baculovirus system typically lack complex biantennary N-linked oligosaccharide side chains containing penultmate galactose and terminal sialic acid residues (Jarvis DL and Finn EE, Nature Biotechnology1996).

For authentic glycosylation modification, our mammalian expression systems provides your best choice.

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