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NDEGLY

Sigma-Aldrich

Native Protein Deglycosylation Kit

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NACRES:
NA.32

conjugate

(N-linked)

Quality Level

200

shipped in

wet ice

storage temp.

2-8°C

Related Categories

General description

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.
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.

Application

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.
Description
  • 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

Storage Class Code

10 - Combustible liquids

WGK

WGK 1

Regulatory Information

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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
Flavio Mena et al.
Neuroendocrinology, 91(1), 77-93 (2009-07-11)
We have previously shown that soluble factor(s) in conditioned media (CM) from the central and peripheral regions of the anterior pituitary (AP) gland of lactating rats promoted the in vitro dose-related release of prolactin (PRL) from pituitary glands of male
Laccase isoform diversity in basidiomycete Lentinus strigosus 1566: Potential for phenylpropanoid polymerization
Kolomytseva MP, et al.
International Journal of Biological Macromolecules (2019)
Adela Rodríguez-Romero et al.
Acta crystallographica. Section D, Biological crystallography, 70(Pt 2), 329-341 (2014-02-18)
Endogenous glycosylated Hev b 2 (endo-β-1,3-glucanase) from Hevea brasiliensis is an important latex allergen that is recognized by IgE antibodies from patients who suffer from latex allergy. The carbohydrate moieties of Hev b 2 constitute a potentially important IgE-binding epitope
Amir E Zeituni et al.
Journal of bacteriology, 192(16), 4103-4110 (2010-06-22)
We recently reported that the oral mucosal pathogen Porphyromonas gingivalis, through its 67-kDa Mfa1 (minor) fimbria, targets the C-type lectin receptor DC-SIGN for invasion and persistence within human monocyte-derived dendritic cells (DCs). The DCs respond by inducing an immunosuppressive and
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O-Linked Glycan Strategies

Learn about O-linked glycan strategies, such as the actions of O-glycosidase, how to remove di and trisialylation sialic acid residues, β-linked galactose, and N-acetylglucosamine, as well as other O-glycan modifications.

Strategies for Deglycosylating N-Linked Glycans

Explore various strategies for deglycosylating N-linked glycans involving PNGase F, PNGase A (Glycopeptidase A), and even native and sequential deglycosylation with endoglycosidases like Endoglycosidase H, Endoglycosidase F, and exoglycosidases.

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