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Glycosylation ts one of the most frequent post-translational modification, playing an essential role m the normal development and physiology of cells. Altered expression of glycans and glycoconjugates has been associated with numerous pathologies, including congenital disorders and cancer. To achieve early diagnosis, cancer biomarkers have been sought for several purposes preferably in blood and pinpointing cancer cells-derived aberrant glycoproteins would be a well-grounded approach to cancer biomarker discovery. One of the glycosyltransferases responsible for aberrant glycosylation m cancer lS N-acetylglucosaminyltransferase v (GnT-V), which catalyzes an addition of betal ,6-N-acetylglucosamine (GicNAc) to the core N-glycan, and many lines of evidence have demonstrated the role of N-acetylglucosaminyltransferase V (GnT-V) in cancer development. Tissue inhibitor of metalloproteinase-1 (TIMP-1) and protein tyrosine phosphatase kappa (PTPk) were suggested to be involved in cancer malignancy upon aberrantly glycosylation by GnT-V. Although cancer biomarker candidates were drived with many lectins and mass spectrometry, an efficient validation method based on a sensitive and multiplexed platform was hampered. Although ELISA-based analytical methods are very powerful for detecting specific proteins, the lectin/antibody sandwich method, which simultaneously recognizes proteins and glycans, is difficult to apply because the antibodies themselves are glycoproteins. To overcome the associated hurdles in this study, antibodies were tagged with oligonucleotides with T7 promoter and then allowed to form a complex with corresponding antigens. An antibody-bound specific glycoform was isolated by lectin chromatography and quantitatively measured on a DNA microarray chip following production of fluorescent RNA by T7-trascription. This tool ensured measurement of targeted glycoforms of multiple biomarkers with high sensitivity and multiplexity, but there are difficulties in cost and reproducibility due to the many steps. Ultimately, in order to overcome this, we have made a mouse that produces a non-glycosylated antibody through a genome editing method, and a recent study on a glycan humanized mouse is also introduced -