Generation of IgG with Sialylated Fc-glycan Profiles using TransGLYCIT®

Performance Activity

Rapid generation of sialylated IgG Fc-glycan profiles, with or without core fucose, for structural and functional characterization.

Sialylated Fc glycans are rather rare on recombinantly expressed mAbs but are found in serum IgGs and have been reported to exert anti-inflammatory effects by regulating the antibody effector functions. Generating defined sialylated IgG glycoforms enables analysis of the impact on antibody structure and function, and the level of Fc glycan sialylation as a potential therapeutic strategy and diagnostic tool for autoimmune diseases. 

Sialylated glycan profiles were generated using the TransGLYCIT platform by remodeling the glycan profile of a therapeutic antibody. The resulting mass spectra after subunit analysis using LC-MS show the glycan profile of trastuzumab, and mass shifts corresponding to transglycosylation of the antibody to generate G2S2 glycoforms or a homogenous afucosylated G2S2 glycan profile.

Simple generation of sialylated Fc-glycoforms with or without core fucose

Generation of IgG with homogeneous G2S2 or G2S2F glycoforms. Deconvoluted mass spectra of the scFc fragment of native trastuzumab (top) and after transglycosylation with TransGLYCIT Remodeling G2S2 (middle), or TransGLYCIT Remodeling Afucosylated G2S2 (bottom). The mAb was digested with FabRICATOR and the subunits analyzed by reversed-phase LC-MS on a Waters™ BioAccord™ system equipped with a Waters™ BioResolve RP mAb column (2.1 x 50 mm).

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