Hydrophilic interaction liquid chromatography (HILIC) is a well-established technique for the separa-tion and analysis of small polar compounds. A recently introduced widepore stationary phase expandedHILIC applications to larger molecules, such as therapeutic proteins. In this paper, we present somegeneric HILIC conditions adapted for a wide range of FDA and EMA approved recombinant monoclonalantibody (mAb) species and for an antibody-drug conjugate (ADC). Seven approved mAbs possessingvarious isoelectric point (pI) and hydrophobicity as well as a cysteine conjugated ADC were used in thisstudy. Samples were digested by IdeS enzyme and digests were further fragmented by chemical reduc-tion. The resulting fragments were separated by HILIC. The main benefit of HILIC was the separation ofpolar variants (glycovariants) in a reasonable analysis time at the protein level, which is not feasible withother chromatographic modes. Three samples were selected and chromatographic conditions were fur-ther optimized to maximize resolution. A commercial software was used to build up retention models.Experimental and predicted chromatograms showed good agreement and the average error of retentiontime prediction was less than 2%. Recovery of various species and sample stability under the appliedconditions were also discussed