Immunoglobulins are heterodimeric proteins composed of 2 heavy and 2 light chains. They
can be separated functionally into variable domains that bind antigens and constant …

Background Glycoproteins and glycolipids exist as an ensemble of glycosylated variants, or
glycoforms. Specific glycoforms are directly modulated by microenvironmental cues and play …

Antibodies play a critical role in linking the adaptive immune response to the innate immune
system. In humans, antibodies are categorized into five classes, IgG, IgM, IgA, IgE, and IgD …

Glycosylation of the Fc region of IgG has a profound impact on the safety and clinical efficacy
of therapeutic antibodies. While the biantennary complex-type oligosaccharide attached to …

IgG molecules are widely used as therapeutic agents either in the form of intact Abs or as Fc
fusion proteins. Although efficient binding of the IgG Fc fragment to cellular FcγRs may be …

A multitude of monoclonal IgG antibodies directed against a variety of therapeutic targets is
currently being developed and produced by biotechnological companies. The biological …

Aims This review is intended to update our previous discussion on the chemoenzymatic
synthesis of carbohydrates and glycoconjugates,(1) with new emphasis placed on …

Immunoglobulin G (IgG) antibodies are important for protection against pathogens and exert
effector functions through binding to IgG-Fc receptors (FcγRs) on myeloid and natural killer …

Breastfeeding is one of the main factors guiding the composition of the infant gut microbiota
in the first months of life. This process is shaped in part by the high amounts of human milk …

The circulatory half-life of recombinant therapeutic proteins is an important pharmacokinetic
attribute because it determines the dosing frequency of these drugs, translating directly to …