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||GE0101||4,000 units; 20,000 units||No||7.5-8.5||Cleaves N-linked glycans without core α1,3 fucose|
|PNGase F-II||GE0201||100 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.