Analysis of Glycopeptides Using MALDImini™-1 Compact MALDI Digital Ion Trap Mass Spectrometer

Many proteins undergo glycosylation. Although these glycans are known to have an important function in regulating protein functions, it is also known that their complex structures and binding states change sensitively due to illness and changes in physical condition. For this reason, it is necessary to clarify the structures of the glycans bound to proteins and their binding sites when researching the relationship between illness and glycoproteins.
This article introduces an analysis using a Shimadzu compact MALDI digital ion trap (DIT) mass spectrometer, focusing on the structure and binding sites of glycans bound to an antibody.

Content Type:
Application
Document Number:
LAAN-A-TM-E070
Product Type:
Mass Spectrometry, Life Science Lab Instruments, MALDI-TOF Mass Spectrometry
Keywords:
Bio-therapeutics, glycan, glycopeptide, digital ion trap, Pharmaceutical, Life Science, MALDImini-1
Language:
English
File Name:
jpo319051.pdf
File Size:
590kb

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For Research Use Only. Not for use in diagnostic procedures.

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