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
| 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 | GE0302 | 5,000 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) |
| FasTEVTM Protease | GE0501 | 1,000 units | No | 6.5-8.0 | Cleaves the peptide bond between a glutamine and a glycine or serine of the consensus sequence ENLYFQ▲G/S |
| Thermophilic Fucosidase | GE0601 | 5,000 units | No | 7.0-7.5 | Cleaves α1,2/3/4/6-linked fucose at high temperature |
| Pan Sialidase | GE0701 | 5,000 units | No | 7.0-7.5 | Cleaves terminal sialic acid |
| Endo S | GE0801 | 2,500 units | No | 5.5-6.5 | Cleaves N-linked glycans from IgG heavy chain |
| β1,3 Galactosidase | GE0901 | 2,000 units | No | 7.5-8.0 | Cleaves terminal β1,3-linked galactose |
| α1,3 Mannosidase | GE1001 | 1,000 units | No | 7.0 | 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).