N-Glycosylation of immunoglobulin G1 (IgG1) at the heavy chain Fc domain (Asn297) plays
an important role for antibody structure and effector functions. While numerous recombinant …

Human immunoglobulins circulate as highly heterogeneously glycosylated mixture of
otherwise homogeneous protein backbones. A series of studies, mainly on IgG, have …

IgG, the main serum immunoglobulin isotype, exists in four subclasses which selectively
appear with distinctive glycosylation profiles. However, very little is known about the …

Production of monomeric IgA in mammalian cells and plant expression systems such as
Nicotiana benthamiana is well-established and can be achieved by co-expression of the …

We investigated N-glycan processing of immunoglobulin G1 using the monoclonal antibody
cetuximab (CxMab), which has a glycosite in the Fab domain in addition to the conserved Fc …

The production of therapeutic antibodies to combat pathogens and treat diseases, such as
cancer is of great interest for the biotechnology industry. The recent development of plant …

N‐glycosylation is critical for recombinant glycoprotein production as it influences the
heterogeneity of products and affects their biological function. In most eukaryotes, the …

Human immunoglobulin E (IgE) is the most extensively glycosylated antibody isotype so
glycans attached to the seven N-glycosites (NGS) in its Fab and Fc domains may modulate …

Proper N-and O-glycosylation of recombinant proteins is important for their biological
function. Although the N-glycan processing pathway of different expression hosts has been …

In recent years, plants have become an attractive alternative for the production of
recombinant proteins. However, their inability to perform authentic mammalian N …