Protein glycosylation is a post‐translational modification often disturbed in cancer.[14] Tumor cells take advantage of these pathways to synthesize aberrant glycans such as the simple truncated O‐glycan sialyl‐Tn (STn),[15, 16] branched N‐glycans, and increased sialylated structures that are reported to confer gastric cancer cells with more aggressive phenotypes and associated with gastric cancer patients’ poor survival.[17, 18] STn is a tumor‐associated antigen expressed in different types of tumors. This evidence concerns the gene EEF1A2 and neoplasm.