Product Overview

PNGase F is the most efficient enzymatic method to remove nearly all N-glycans from glycoproteins. PNGaseF digests the glycosidic bond between the innermost N-acetylglucosamine and asparagine residues. It cleaves N-glycans attached to glycoproteins, including high-mannose, hybrid, and complex oligosaccharide glycoforms.

Key Features

Efficient N-glycan release enzyme

PNGase F is widely used for enzymatic removal of N-linked glycans from glycoproteins by cleaving the bond between the innermost N-acetylglucosamine and asparagine residues. It is applicable to high-mannose, hybrid, and complex N-glycan structures.

Preservation of glycan core structure

After enzymatic digestion, the released N-glycans retain their core structures, making them suitable for downstream structural and analytical studies.

High purity

Purity is typically ≥95% as determined by standard analytical methods.

Flexible reaction conditions

Compatible with both denaturing and non-denaturing digestion conditions depending on experimental requirements.

Multiple product formats available

Different enzyme formats are available to support diverse application needs (e.g., HBP003006/ HBP003013 /HBP003004).

Applications

N-glycan release for structural analysis

Used for enzymatic cleavage of N-linked glycans prior to downstream analytical workflows, typically performed at 37 °C under recommended conditions.

CE and chromatography-based glycan analysis

Suitable for sample preparation in capillary electrophoresis (CE), HPLC, or LC-MS-based N-glycan profiling methods.

Glycoprotein characterization

Applied in glycoprotein analysis workflows to support structural and comparative glycosylation studies.

FAQ

What components are included in the PNGaseF system?

The product system typically includes PNGaseF enzyme, 10× Glycoprotein Denaturing Buffer, 10×GlycoBuffer2, and 10% NP-40, supporting both denaturing and non-denaturing deglycosylation workflows.

Protocols under denaturing and non-denaturing conditions