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PNGase F from Yinjia Bio is recombinantly expressed in Escherichia coli. It selectively hydrolyzes all Asn-linked N‑glycans on glycoproteins except those containing an α1‑3 fucosidic linkage. The cleavage takes place between the asparagine residue and the innermost GlcNAc, releasing Asn‑linked glycans from glycoproteins and converting asparagine to aspartic acid. The enzyme is active on high‑mannose, hybrid, and complex oligosaccharides.
Product images are for reference only.
Applications
Complete removal of N-glycans from antibodies and glycoproteins.
Advantages
(1) High purity: Free of other protease contaminations; no endo- or exo-glycosidase activities; purity ≥ 95%.
(2) High stability: Each batch undergoes strict quality control to ensure batch-to-batch consistency.
(3) High specific activity: Efficient and complete release of N-linked glycans.
(4) Compatible with downstream HPLC and MS: Glycerol-free PNGase F helps achieve optimal results in downstream analysis.
(5) Flexible reaction conditions: Can deglycosylate glycoproteins under both denaturing and native conditions.
Information
PNGase F, Liquid, With Glycerol
(1) Product Name: PNGase F
(2) Catalog No. : YJ-O-071
(3) Size: 15 KU / 20 KU / 40 KU
PNGase F, Lyophilized
(1) Product Name: PNGase F, Lyophilized
(2) Catalog No. : YJ-O-133
(3) Size: 15 KU / 20 KU / 40 KU
PNGase F, Liquid, Glycerol-free
(1) Product Name: PNGase F (glycerol-free)
(2) Catalog No. : YJ-O-252
(3) Size: 15 KU / 20 KU / 40 KU / 5× 15 KU / 75 KU