The Thermo Scientific Vanquish UHPLC system with Fluorescence detection is applied for the rapid glyco-profiling of a commercial chimeric IgG1 mAb.The separation is performed on a Thermo Scientific Accucore-150-Amide HILIC column in under 2.5 minutes. The developed methodology offers an excellent analytical platform for ultrafast glycan profile comparison of different batches​ of these mAbs.

The Thermo Scientific Vanquish H system with fluorescence detection is applied for the rapid glycoprofiling of a commercial chimeric IgG1 mAb. The separation is performed on a Thermo Scientific Accucore-150-Amide HILIC column in under 2.5 minutes. Developed methodology offers an excellent analytical platform for ultrafast glycan profile comparison of various production batches.

The Thermo Scientific Vanquish H UHPC with Fluorescence detection is applied for the glycan profile comparison of trastuzumab innovator to a biosimilar candidate produced ‘in house’ using Chinese hamster ovary (CHO) cell line using HILIC-based chromatographic separation on Accucore 150-Amide-HILIC column. Developed methodology offers an excellent analytical platform for glycan profile comparison of multiples lots of both the innovator and biosimilar products

The Thermo Scientific Vanquish H UHPLC system was used for the high resolution determination of 2-AA (anthranilic acid) labelled N-glycans released from a commercial chimeric IgG1 mAb (Infliximab). The separation is performed on a 150 mm Accucore 150-Amide-HILIC column with fluorescence detection giving separation in less than 30 minutes.N-Glycans present at the asparagine 297 residue in the CH2 domain of the Fc region of IgG play a crucial role in modulating the structural stability and functional activity relationship of the antibody.

The Thermo Scientific Vanquish H UHPLC system is applied for the rapid determination of 2-AB (2-aminobenzamide) labelled N-glycans released from human serum IgG in less than 15 minutes using a 50 mm Thermo Scientific Accucore 150-Amide-HILIC column with fluorescence detection. The method is able to determine N-Glycans present at the asparagine 297 residue in the CH2 domain of the Fc region of IgG that play a crucial role in modulating the structural stability and functional activity relationship of the antibody.