N-Zyme Products 

PNGase F PRIME™ GLYCOSIDASE (Liquid Format)

This enzyme is a proprietary mutant recombinant PNGase F, cloned from Flavobacterium meningosepticum and expressed and purified from E. coli. Excellent for use in high-end use applications especially those using or requiring UPLC/HPLC, Hydrophilic Interaction Chromatography (HILIC), and/or MALDI-Glycan Mass Spec Imaging. 1 Unit of enzyme will completely deglycosylate 10 µg of denatured RNase B following incubation for 10 minutes at 37°C. Impact on protein can be visualized by SDS-PAGE. Released glycans can be examined following labeling with the Waters RapiFluor-MS dye and analyzed by normal phase hydrophilic interaction chromatography (HILIC) using various HPLC/UPLC-based systems. Imaging of released glycans directly on tissue can be done following spraying of enzyme on tissue and incubation at 37°C for 1 hour. (At our standard concentration of 2mg/mL, one 50 µL vial can make 4 slides.) Glycans can be detected using instruments such as the Bruker Daltonics SolariX™ 7T Hybrid FTMS System, a Bruker Daltonics RapifleXTM MALDI Tissuetyper, or a Bruker Daltonics UltrafleXtreme MALDI-TOF/TOF mass spectrometer.

PNGase F PRIME-LY™ GLYCOSIDASE (Lyophilized Format)

PNGase F PRIME-LY™ Glycosidase is the same enzyme as our standard liquid format PNGase F PRIME™ but now available in a lyophilized form, which is perfectly suitable for use in solution-based analyses. Performance characteristics and applications in which it can be used remain exactly the same as with our standard liquid format PNGase F PRIME™ enzyme. This enzyme specifically removes N-linked oligosaccharides from glycoproteins.

PNGase F PRIME-LY™ ULTRA GLYCOSIDASE (Lyophilized Format)

PNGase F PRIME-LY™ ULTRA Glycosidase is optimized and specifically formulated for high resolution imaging in small structures or cells. This enzyme specifically removes N-linked oligosaccharides from glycoproteins. This is a high-performance enzyme that has been shown to require as few as 3,000 cells per replicate with 3-20% coefficient of variation to capture label-free N-glycan profiles (as shown in Angel et. al., J Proteome Res. 2019).

Endo F3 PRIME-LY™ (Lyophilized Format)

Endo-β-N-acetylglucosaminidase F3 (Endo F3) cleaves in β(1-4) link in between the two core GlcNAcs of asparagine linked glycans. Endo F3 cleaves this link on core-fucosylated structures. Endo F3 can be applied to workflows alone or in conjunction with PNGase F PRIME™ to allow for structural characterization of core-fucosylated glycans in tissues while maintaining spatial localization. Endo F3 PRIME-LY™ comes in a lyophilized format that is perfectly suitable for use in solution-based analyses. 

Endo S PRIME-LY™ (Lyophilized Format)

Endo-β-N-acetylglucosaminidase S (Endo S) cleaves the hydrolysis of the β(1-4) linkage between the two core GlcNAcs of asparagine linked biantennary complex-type glycans of IgG Fc regions. This endoglycosidase only deglycosylates IgG glycoforms and plays a central role in glycoengineering strategies for the development of IgG antibodies with improved therapeutic efficacy. Endo S PRIME-LY™ comes in a lyophilized format that is perfectly suitable for use in solution-based analyses.

Sialidase PRIME-LY™ (Lyophilized Format)

Sialidases are a family of exoglycosidases that catalyze the cleavage of non-reducing sialic acid residues of mono- or oligosaccharide chains on glycoconjugates. Sialidase PRIME-LY™ comes in a lyophilized form, which is perfectly suitable for solution-based analyses. This enzyme cleaves α2,3-, α2,6- and α2,8- linked sialic acids. Because of its broad substrate specificity, Sialidase PRIME-LY™ is capable of completely removing sialic acids from glycoconjugates of a wide variety of biological materials (cells, antibodies, serum, tissues etc.).