Amerigo Scientific introduces the launch of Recombinant PNGase F enzyme for release of N-linked glycans in solution, and from immobilized samples. It is noted that this new enzyme is for research use only, and is not for human or drug use.
Enzymes are biological catalysts that regulate the rate of chemical reactions that proceed in organisms and play irreplaceable roles in signal transduction pathways and cell regulation pathways. Amerigo Scientific offers a comprehensive collection of enzymes from global manufacturers covering all the core biological research areas. This Recombinant PNGase F enzyme is now newly released for researchers all over the world.
LudgerZyme Peptide N-glycosidase F (PNGase F) is suitable for release of N-linked glycans in solution, and from immobilized samples. This enzyme cleaves between the innermost GlcNAc of the oligosaccharide moiety at its attachment point to the asparagine residue on the protein and subsequently converts the asparagine into aspartic acid. Released glycans with free reducing terminus can be labelled using LudgerTag labelling technology for fluorescence and high MS sensitivity detection.
LudgerZyme PNGase F (EC 3.5.1.52) is a recombinant glycosidase cloned from Elizabethkingia miricola and expressed in E. coli. The enzyme is supplied glycerol free (for optimal performance in HPLC intensive methods) along with Reaction Buffer, Denaturation Solution and NP-40 Solution for efficient de-glycosylation. PNGase F is suitable for release of all types (high-mannose, hybrid and complex) N-linked glycans from glycoproteins and glycopeptides. PNGase F will not remove oligosaccharides containing a(1-3) linked core fucose commonly found on plant glycoproteins. Xaa-Asn-Xaa sequence is the minimal peptide substrate for this enzyme. Some non-mammalian glycans from sources such as plants, insects and parasites carrying a1-3 linked core fucose will not be cleaved with PNGase F. For these samples PNGase A can be used.
enzymes