Glycoproteomics aims at the concomitant identification of not only the composition of the glycan but also the sites of glycosylation and the determination of the protein attached with glycans. However, glycopeptide analysis is challenging because their microheterogeneity results in the reduced concentration of each individual glycopeptide molecule compared to unmodified peptides, even if they are obtained from the very same digest sample (1). Also, glycopeptides exhibit poor ionization efficiency compared to their nonglycosylated counterparts (2). Therefore, it is essential to perform selective and efficient glycopeptide enrichment by solid-phase extraction (SPE) prior to detection and identification by mass spectrometry (MS) analysis (3–10). Hydrophilic interaction liquid chromatography (HILIC) SPE has been extensively applied in the past decade because of its low bias towards different glycan types (9,10). In contrast to normal‑phase liquid chromatography, the HILIC retention mechanism is mainly based on the hydrophilic partitioning of the analyte to the enriched superficial water layer surrounding the surface of the polar stationary phase (11). Ionic interaction and hydrogen bonding may also be involved in the separation depending on the sample properties and the character of HILIC stationary phase. Here, we demonstrate the glycopeptide enrichment efficiency of iSPE®-HILIC material for glycoproteomics applications using a well characterized glycoprotein standard.