Glycosylation, the post-translational modification of a protein, lipid, or nucleic acid with specific carbohydrate chains, is a widespread phenomenon in biology. The two most common forms are N– and O-glycosylation, and the glycans can have significant effects on the properties of the biomolecule. Analysis of glycans is typically done through glycan removal or trimming using endo and/or exo-glycosidases, followed by downstream assays.
Lectenz Bio offers a suite of glycan processing enzymes. These include enzymes PNGase F, PNGase F-II, α2,3 Sialidase, and O-GlcNAcase.
Glycan Processing Enzymes
|4,000 units; 20,000 units
|Cleaves N-linked glycans without core α1,3 fucose
|Cleaves N-linked glycans with or without core fucose, both α1,6 and α1,3
|Cleaves terminal α2,3-linked sialic acid
|Cleaves O-linked β-N-Acetylglucosamine (GlcNAc)
|Cleaves the peptide bond between a glutamine and a glycine or serine of the consensus sequence ENLYFQ▲G/S
|Cleaves α1,2/3/4/6-linked fucose at high temperature
|Cleaves terminal sialic acid
|Cleaves N-linked glycans from IgG heavy chain
|Cleaves terminal β1,3-linked galactose
|Cleaves terminal α1,3-linked mannose
Glycoproteins digested with Lectenz Bio PNGase F or PNGase F-II. A. PNGase F is commonly used to cleave N-glycans from mammalian proteins with or without α1,6-core fucosylation, such as bovine ribonuclease B (RNase B). B. PNGase F-II can also cleave RNase B, as well as α1,3-core fucosylated N-glycans from insect or plant proteins, such as horseradish peroxidase (HRP).