N-glycosylaNon is a common PTM observed in biotherapeuNc proteins . This modificaNon plays a criNcal role in protein folding, efficacy and immunogenic response of the molecule and hence regulatory agencies require rigid control and analysis of this PTM . For the here invesNgated molecule, N-glycosylaNon was observed at N126 residue. The relaNve abundances of various N-glycans are detailed in Figure , where most abundant structures correspond to core fucosylated structures. The main glycoform observed was A2G0F which is the core fucosylated agalactosyl biantennary glycan which consNtutes >85% of the total N-glycosylaNon with relaNve abundances ranging from 86.48% to 87.64% for the DS reference material and four commercial DP batches. The second most dominant glycoform observed was A2G1F, core fucosylated mono galactosyl biantennary glycan which yielded abundance levels between 2.80% and 4.62%. The presence of high mannose glycans have been observed to result in reduced complement dependent acNvity and an increase in serum clearance in humans and mice . The levels of high mannose glycans can vary from molecule to molecule but for commercial biotherapeuNcs the acceptable level is <10% . For the GLCP Fc-fusion protein, M5 was observed at an abundance ranging from 0.54% to 0.69% for the four commercial batches and reference standard material. Sialylated glycoforms were also detected at lower abundance. The data is visualised in Figure .