CD BioGlyco is a world-leading independent biotechnology company, focusing on high-quality innovative Antibody Digestion Services. Our advanced technology platforms and high-quality services will fully meet your needs for the digestion of IgG in the hinge region. We have the confidence to be your essential research assistant in the field of antibody glycoengineering.
IgG monoclonal antibodies require the synergy of the antigen binding and Fc (effector) domains for their efficient function in the removal of pathological cells. The hinge regions linking these domains exhibit binding effects to Fc receptors on immune effector cells, resulting in pathological cell lysis. In recent years, proteolytic enzymes with no negative impact on human physiology have been successfully used to generate IgG fragments for reagent and therapeutic use. It was subsequently noted that proteases also cleaved human IgG specifically in the hinge region.
Pepsin-mediated digestion allows different sites in the hinge to split IgG, resulting in producing a fragment that contains two binding sites F(ab')2. This fragment is cleaved into two identical univalent fragments that are almost identical with Fab. FC fragments generated by pepsin digestion are usually unable to recover.
Fig.1 A representative image of a human IgG1 antibody is on the left side with the hinge region amino acids on the right.
(Brezski & Jordan, 2010)
CD BioGlyco provides a protease that digests IgG in the hinge region. The protease digests the hinge regions of antibodies including human IgG1-4 and IgG from mice, rats, goats, sheep, and rabbits. Fab and Fc fragments are produced after digestion.
CD BioGlyco has developed an advanced Glycoengineering Platform for research in glycoscience. Our professional research teams provide customers with high-quality services for the digestion of IgG in the hinge region according to your needs. If you are interested in our services, please contact us for more details without any hesitation.
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