This product is a mixture of five recombinant enzymes expressed in Escherichia coli:

PNGase F selectively hydrolyzes all Asn-linked N‑glycans on glycoproteins except those containing an α1‑3 fucosidic linkage. The cleavage takes place between the asparagine residue and the innermost GlcNAc, releasing Asn‑linked glycans from glycoproteins and converting asparagine to aspartic acid. The enzyme is active on high‑mannose, hybrid, and complex oligosaccharides.

O-Glycosidase is also known as endo-α-N-acetylgalactosaminidase. After removal of terminal sialic acid residues from glycoproteins with sialidase, O-Glycosidase catalyzes the removal of O-linked disaccharides with core 1 and core 3 structures from glycoproteins. This product is glycerol-free in storage buffer, ensuring excellent compatibility with downstream mass spectrometry and HPLC. It contains a His-tag for convenient removal via chromatography.

α2-3,6,8,9 Neuraminidase hydrolyzes sialic acids linked via α2-3, α2-6, α2-8 and α2-9 glycosidic bonds on glycoproteins and oligosaccharides. The hydrolysis rate for α2-3 and α2-6 linkages is higher than that for α2-8 and α2-9 linkages.

β1‑4 Galactosidase is a highly specific exoglycosidase that catalyzes the hydrolysis of non‑reducing terminal galactose residues from oligosaccharides.

β-N-Acetylhexosaminidase catalyzes the hydrolysis of terminal β-D-N-acetylgalactosamine and glucosamine residues from oligosaccharides, and can be used to remove O-GlcNAc.

Product images are for reference only.