Native Protein Deglycosylation Kit

Pricing and availability is not currently available.

Quality Level

shipped in

wet ice

storage temp.


Related Categories

General description

The Native Protein Deglycosylation is designed for the deglycoslylation of N-linked oligosaccharides from PNGase F-resistant native proteins. Endoglycosidases F1, F2, and F3 are less sensitive to protein conformation than PNGase F and are more suitable for removal of all classes of N-linked oligosaccharides without protein denaturation.
All complex oligosaccharides can be reduced to the trimannosylchitobiose core by treatment of the glycoproteins with neuraminidase, β-galactosidase, and N-acetylglucosaminidase. Fucosidases may be required in some situations. The remaining trimannosylchitobiose core structures can be removed with endoglycosidase F3. Biantennary and triantennary structures can be immediately removed by endoglycosidases F2 and F3, respectively. Oligomannose and hybrid structures can be removed by Endoglycosidase F1.
For more information on each type of endoglycosidase, please refer to the Bulletin.


Native Protein Deglycosylation Kit has been for N-deglycosylation of various enzymes such as laccase, tomato nuclease TBN1 and endo-β-1,3-glucanase.

Storage and Stability

The NDEGLY Kit ships on wet ice and storage at 2–8 °C is recommended. This kit may be used for at least 1 year when stored as indicated. Several days exposure to ambient temperatures will not reduce the activity of the enzymes in this kit.

Kit Components Only

Product No.

  • Endoglycosidase F1 .3 U

  • Endoglycosidase F2 .1 U

  • Endoglycosidase F3 .1 U

  • Endoglycosidase F1 reaction buffer 200 μL

  • Endoglycosidase F2 & 3 reaction buffer 200 μL


NONH for all modes of transport

N-glycosylation of tomato nuclease TBN1 produced in N. benthamiana and its effect on the enzyme activity
Podzimek T, et al.
Plant Science (2018)
Laccase isoform diversity in basidiomycete Lentinus strigosus 1566: Potential for phenylpropanoid polymerization
Kolomytseva MP, et al.
International Journal of Biological Macromolecules (2019)
Chaouki Benabdessalem et al.
Biochemical and biophysical research communications, 516(3), 845-850 (2019-07-03)
We previously reported that immunoreactivity of recombinant CFP32 (Rv0577), a virulence factor of Mycobacterium tuberculosis, was higher when produced in transformed Pichia pastoris as compared to transformed E. coli. In this study, we show that this difference is partly due to...
M P Kolomytseva et al.
International journal of biological macromolecules, 137, 1199-1210 (2019-07-12)
Three laccase isoforms with different physicochemical properties could be purified from culture liquid of basidiomycete Lentinus strigosus 1566 obtained during submerged cultivation. The purified laccases possessed individual selectivity in relation to different phenolic compounds. Laccases I, II, and III (59...
There is no enzyme comparable to PNGase F for removing intact O-linked sugars. Monosaccharides must be sequentially hydrolyzed by a series of exoglycosidases until only the Gal-b(1-3)-GalNAc core remains. O-Glycosidase can then remove the core structure intact with no modification of the serine or threonine residue.
Read More
Deglycosylation Kits
Read More
Post-translational modifications such as glycosylation, phosphorylation, and sulfation, to name a few, serve many functions. As a result, the analysis of proteins and their post-translational modifications is particularly important for the study of diseases where multiple genes are known to be involved, such as heart disease, cancer and diabetes.
Read More

Our team of scientists has experience in all areas of research including Life Science, Material Science, Chemical Synthesis, Chromatography, Analytical and many others.

Contact Technical Service

Social Media

LinkedIn icon
Twitter icon
Facebook Icon
Instagram Icon


Research. Development. Production.

We are a leading supplier to the global Life Science industry with solutions and services for research, biotechnology development and production, and pharmaceutical drug therapy development and production.

© 2021 Merck KGaA, Darmstadt, Germany and/or its affiliates. All Rights Reserved.

Reproduction of any materials from the site is strictly forbidden without permission.