Description
PNGase F is an enzyme used in biochemistry and molecular biology to remove N-linked glycans from glycoproteins. By using PNGase F, researchers can enzymatically cleave between these sugar chains and asparagine residues of glycoproteins, allowing for the study of protein structure and function, particularly in glycosylation research.
Components
10X Glycoprotein Denaturing Buffer
1 vial (1 mL)
10X Reaction buffer
1 vial (1 mL)
10% NP-40
1 vial (1 mL)
Expression system
Escherichia coli
Concentration
400 U /μL
Buffer
20mM Tris-HCl, 50mM NaCl, 5mM EDTA, pH 7.5
Purity
>95% as determined by SDS-PAGE analysis.
Unit Definition
One unit is defined as the amount of enzyme required to remove > 95% of the carbohydrate from 10 µg of denatured RNase B in 1 hour at 37°C in a total reaction volume of 20 µL.
Endotoxin level
<0.05 EU per 1 µg of the protein by the LAL method.
Mycoplasma
Not detected
Form
Liquid
Stability & Storage
This product is stable after storage at:
Manufacturing specifications
LeadGMP® recombinant proteins are manufactured in ISO 13485:2016 and GMP certified facility. The processes include:
The intracellular PD-L1 protein was digested with LeadGMP® PNGase F and analyzed by Western blotting. The assay was performed by incubating 400 U PNGase F and 20 µg of glycoprotein from whole cell lysate.
SDS-PAGE analysis of recombinant PNGase F
PNGase F cleaves high mannose, hybrid-type and complex structure glycans.
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