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IMPa is a broad-specificity metalloprotease that selectively cleaves peptide bonds on the N-terminal side of serine or threonine residues bearing mucin-type O-linked glycans. It has become an essential tool in glycoproteomic workflows, enabling site-specific analysis of O-glycosylation and facilitating the structural characterization of mucin-type glycopeptides -
Neuraminidase A (NanA) from Streptococcus pneumoniae cleaves terminal α2-3 and α2-6 sialic acids from glycoconjugates, exposing underlying sugars. It is used for glycoprotein/glycan analysis, biopharmaceutical desialylation, and enzymatic synthesis or modification of glycoconjugates. -
Neuraminidase B (NanB) from Streptococcus pneumoniae selectively cleaves terminal α2-3-linked sialic acids from glycoconjugates and can generate 2,7-anhydro-Neu5Ac through its transglycosidase-like activity. It is used for linkage-specific glycoprotein/glycan analysis, controlled desialylation in bioprocessing, production of analytical sialic-acid standards, and enzymatic synthesis or modification of glycoconjugates.
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Neuraminidase C (NanC) from Streptococcus pneumoniae selectively cleaves terminal α2-3-linked sialic acids with limited activity toward α2-6 linkages, releasing free sialic acid. Its mild, controlled desialylation makes it useful for glycoprotein/glycan structural analysis, biopharmaceutical desialylation, production of analytical sialic-acid standards, and enzymatic synthesis or modification of glycoconjugates
