Glycostation Profile of IgGs Using a Linear Benchtop MALDI-TOFMS and Affinity Purification of Fc

Glycosylation on protein plays wide-range vital roles in biological processes from the stabilization of protein conformation to the expression of binding specificity. In this view, a characterization of the N-/O-linked glycan is rather significant, especially in the development of biopharmaceuticals. To date, whereas intensive efforts have been conducted on the precise characterization of glycans with high-end mass spectrometers, inexpensive easy-to-use commercial instruments have been anticipated for batch analysis assuming screening or quality assurance/quality control (QA/QC). A newly developed bench-top MALDI-TOFMS, MALDI-8020, is expected to be a suitable instrument in terms of sufficient specification, through-put, and cost effectiveness. We attempted to characterize the glycosylation of IgG using the MALDI- 8020 without a release of glycan. To this end, we examined a quick preparation using affinity beads and enzymatic cleavage.

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Life Science
glycostation, IgGs, Linear benchtop maldi, affinity purification of lc, Pharma & Biopharma, Monoclonal Antibodies and Biosimilars, MALDI-8020
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