The gastric cancer is the fourth most common cancer and the second most common cause of cancer related death worldwide, particularly prevalent in many Asian countries, especially China. Protein glycosylation is one of the most common posttranslational modifications made to proteins. Glycans can be attached to proteins either via an amide group or a hydroxyl group, which occur through different biosynthetic pathways and potentially have independent functions. N-linked glycosylation plays fundamental roles in many biological processes such as cell adhesion, cell migration, and signal transduction. Abnormal expression of N-linked glycoproteins has been observed in various diseases. Upon in-depth characterization of N-linked glycoproteins and disease-associated glycosylation changes, several methodologies have been developed. In our previous study, we have identified some N-glycan markers in heptatocellular carcinoma and colon cancer using a capillary based electrophoresis called DNA sequencer-assisted fluorophore-assisted capillary electrophoresis. In addition, it has been reported that a-1, 6-fucosyltransferase activity and expression is increased in several human cancers, suggesting a role for this enzyme in tumor development and progression, such as HCC, colorectal cancer, nonsmall cell lung cancer and ovarian serous adenocarcinoma. Altered core-fucosylation is one of the most important abnormal glycosylated modification identified in malignancies. Fut8 catalyzes the transfer of fucose from guanosine diphosphate -fucose to the innermost GlcNAc of hybrid and complex N-linked oligosaccharides via an a-1,6-linkage, resulting in core-fucosylated glycoproteins and altering biological function of resulting glycoproteins. Although many studies have reported the association between altered core-fucosylation and other aggressive tumors, to our knowledge, the influence of core-fucosylation on gastric cancer remains unknown. In this study, we analyzed N-glycan profiling with DSA-FACE in both serum samples from gastric cancer, gastric ulcer, healthy controls and tissue proteins from tumors and adjacent non-tumors. Then extend the functional research upon the identified specific glycosylations. Glycosylation is one of the most common post-translational modifications appeared in about 70% of all known proteins. Alterations in glycosylation play a role in a diverse set of biological phenomena such as tumor cell metastasis, intracellular communication and inflammation. More and more studies indicate that the alterations of glycosylation and the levels of glycosyltransferases activities derived from the malignant transformation are relevant to human malignancies. DSA-FACE is a simple and efficient technology for measuring N-glycan changes in serum. We previously used this technology to assist in the diagnosis of HCC and CRC. In the current study, we used it to analyze characteristic N-linked profiling pattern in gastric cancer.