PNGase F 

PNGase F, a glycosidase, catalyzes the cleavage of an internal glycoside bond in an oligosaccharide. PNGase F removes nearly all N-linked oligosaccharides from glycoproteins. PNGase F can release N-glycans from glycoproteins in glycoanalytical workflows^[1][2].

Application: 1. In vitro de-glycosylation modification of antibodies, immunoglobulin fusion proteins or other glycoproteins; 2. Characterization of whether there is N-glycosylation modification in proteins.

molecular weigh: 36 kDa
optimal temperature: 37 ℃
pH range:6.0-10.0
temperature range: 4-50 ℃
ionic strength range: 0-1 M NaCl
PNGase F storage solution: 10 m M Tris (pH7.4), 50 m M NaCl, 5 m M EDTA. The storage solution does not contain glycerol, making it easier to optimize chromatographic conditions for HPLC methods.
Reaction Buffer (10X): 500 m M Sodiu M Phosphate (pH7.5)

PNGase F cannot hydrolyze N-glycosides containing core α 1-3 fucose, which are common in plant and insect glycoproteins. In this case, PNGase A needs to be used.

MedChemExpress (MCE) has not independently confirmed the accuracy of these methods. They are for reference only.

83534-39-8

Liquid

Colorless to light yellow

[PNGase F]

Room temperature in continental US; may vary elsewhere.

Please store the product under the recommended conditions in the Certificate of Analysis.

• [1]. Vilaj M, et al. Evaluation of different PNGase F enzymes in immunoglobulin G and total plasma N-glycans analysis. Glycobiology. 2021 Jan 9;31(1):2-7.  [Content Brief]

  [2]. Huang J, et al. Highly Efficient Release of Glycopeptides from Hydrazide Beads by Hydroxylamine Assisted PNGase F Deglycosylation for N-Glycoproteome Analysis. Anal Chem. 2015 Oct 20;87(20):10199-204.  [Content Brief]