Endo-beta-N-acetylglucosaminidase F3 (Endo F3) from Flavobacterium Meningosepticum N-glycans are commonly found on various glycoproteins. While peptide N-glycosidase from Flavobacterium meningosepticum (PNGase F) is widely used to release virtually all types of N-glycans under denaturing conditions, endo-beta-N- acetylglucosaminidases from the same bacterial species can be used under native conditions to specifically release particular types of N-glycans (1, 2). Because these glycosidases hydrolyze the chitobiose core of N-glycans, the released glycan products will contain one GlcNAc residue at their reducing ends with the other GlcNAc residue remaining attached to the asparagine residue on the glycoproteins. Endo F3 hydrolyzes bi- and triantennary N-glycans (3). In general, this enzyme is more efficient on core fucosylated N-glycans increasing activity up to 400-fold with biantennary structures (4). It also cleaves fucosylated trimannosyl core structures.