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Cat. No.: PNGFH-15k

Cat. No.: PNGFH-75k

Description

PNGase F (Peptide N-Glycosidase F) originates from Elizabethkingia miricola and is an efficient amidase hydrolyzing enzyme. It can cleave high mannose, hybrid, and complex oligosaccharide glycoproteins linked by asparagine. The cleavage site of PNGase F is the amide bond between the inner N-acetylglucosamine (GlcNAc) of the glycoprotein and the asparagine residue, simultaneously converting the asparagine residue to aspartic acid after enzymatic hydrolysis. This product is expressed via recombinant expression in Escherichia coli, with a His tag, without glycerol, commonly used for deglycosylation of antibodies and related proteins. Avoid repeated freeze-thaw cycles during use.

Unit Definition

One enzyme activity unit (U) refers to the amount of enzyme required to remove more than 95% of carbohydrates from 10 μg of denatured RNase B in a 10 μl reaction system at 37°C for 1 hour.

Inactivation Conditions

Incubation at 75°C for 10 minutes.

Quality Control

• Protein Purity Analysis: Assessed using SDS-PAGE gel electrophoresis, protein purity is not less than 95%.
• Glycosidase and Protease Activity Assay: No detectable endonuclease F1, F2, or F3 activity; no detectable protease activity.

PNGase F Removal

This product carries a His tag and, after reaction, can be removed by affinity chromatography using a different tag from the target glycoprotein.

Storage

Store at -20ºC.

Related: 

• PNGase F
• PNGase F (with His-tag)
• PNGase F (with His-tag, Glycerol Free)
• PNGase F Deglycosylation Kit with Magnetic Beads
• Rapid PNGase F Deglycosylation Kit (Denaturing Method)
• Rapid PNGase F Deglycosylation Kit (Native Method)

Only for research and not intended for treatment of humans or animals

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