Glycan Processing

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 substitution of different glycans can have significant effects on the properties of the ligand. Analysis of glycans is typically done through glycan trimming or removal 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

Product Name Catalog Number Amount Glycoprotein? Optimal pH Activity
PNGase F GE01014,000 units; 20,000 units No 7.5-8.5 Cleaves N-linked glycans without core α1,3 fucose
PNGase F-II GE0201100 units No 6.5-7.5 Cleaves N-linked glycans with or without core fucose, both α1,6 and α1,3
α2,3 Sialidase GE0301 5,000 units; 50,000 units No 7.0-7.5 Cleaves terminal α2,3-linked sialic acid
O-GlcNAcase GE0401 1,000 units No 7.5 Cleaves O-linked β-N-Acetylglucosamine (GlcNAc)

Glycoproteins digested with Lectenz Bio PNGase F or PNGase F-II. PNGase F is the standard enzyme for N-Glycan removal, whereas PNGase F-II is able to cleave N-Glycans from plants and insects that have an ⍺-fucosylated core.