Custom Glycosylation of Antibodies

Custom Glycosylation of Antibodies

CD BioGlyco has been committed to providing customers with high-quality glycosylation services of antibodies. Our services include custom antibody glycosylation modifications and antibody glycosylation analysis. Welcome customers from all over the world to cooperate with us!

Glycosylation of Antibodies

Antibodies are key components of protective immune responses in many diseases, serving as cell-associated and soluble receptors for foreign substances. Antibodies are composed of variable domains (F(ab')2) and constant domains (Fc). Among them, F(ab')2 is responsible for recognizing antigens, and the Fc region interacts with different Fc receptors and complement proteins. Antibody glycosylation is a common post-translational modification that plays a key role in antibody effector function. Interest in antibody glycosylation has exploded in recent years, in part due to the rapid expansion of therapeutic antibody repertoires. To achieve the desired therapeutic effect, antibodies with specific glycoforms are produced by glycoengineering.

Composition of complex-type N-linked glycan on IgG.Fig.1 Composition of complex-type N-linked glycan on IgG. (Shade, 2013)

Structure of Fc Core Glycan

Monoclonal antibodies trigger effector functions after binding to antigen molecules. The effector functions are mediated by the Fc. The binding of Fc to Fc receptors or related complement proteins triggers antibody-dependent cell-mediated cytotoxicity (ADCC) or complement-dependent cytotoxicity. (CDC). The glycosylation level of the Fc of the monoclonal antibody affects ADCC and CDC and changes the pharmacokinetic properties of the antibody. Part of the glycoform structure also affects the immunogenicity of the antibody. The structure of the Fc core glycan is a complex "biantennary" pentasaccharide molecule composed of three mannose (Man) and two N-acetylglucosamine (GlcNAc) molecules. And different glycoforms may contain various amounts of other molecules such as fucose (Fuc), Man, N-GlcNAc, galactose (Gal), bisecting GlcNAc, and sialic acid (Sia).

Our Glycosylation Services of Antibodies

  • Modification of antibody glycosylation

Glycosylation modifications affect the immunogenicity, half-life, and effector factors of therapeutic drugs. For example, the absence of Fuc modification enhances ADCC activity, while sialylation affects the anti-inflammatory properties of monoclonal antibody (mAb) molecules. CD BioGlyco has different glycosylation technologies and provides customers with a series of antibody glycosylation services, including fucose deficiency, sialylation, etc.

  • Characterization of antibody glycosylation

In addition, CD BioGlyco provides antibody glycosylation analysis services through a variety of methods, such as capillary electrophoresis (CE), high-performance liquid chromatography (HPLC), electrospray ionization mass spectrometry (ESI-MS), Fourier ion cyclotron resonance mass spectrometry (FT-ICR-MS), size exclusion chromatography (SEC), and matrix-assisted laser desorption ionization-time of flight mass spectrometry (MALDI-TOF MS).

CD BioGlyco provides high-quality, cost-effective, and hassle-free custom glycosylation of antibodies. If you are interested in our services, please feel free to contact us, we are looking forward to being your indispensable assistant in the glycosylation field.


  1. Irvine, E.B.; Alter, G. Understanding the role of antibody glycosylation through the lens of severe viral and bacterial diseases. Glycobiology. 2020, 30(4): 241-253.
  2. Shade, K.T.; Anthony, R.M. Antibody glycosylation and inflammation. Antibodies. 2013, 2(3): 392-414.
This service is for Research Use Only, not intended for any clinical use.

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