Skip to Content
Merck
CN
All Photos(1)

Documents

Safety Information

EMS0001

Sigma-Aldrich

PNGase Fast

recombinant, expressed in E. coli

Synonym(s):

N-Glycosidase F, PNGase F, Peptide N-glycosidase

Sign Into View Organizational & Contract Pricing


About This Item

UNSPSC Code:
41131616

recombinant

expressed in E. coli

Quality Level

conjugate

(N-linked)

grade

Proteomics Grade

form

ready-to-use solution

shipped in

wet ice

storage temp.

2-8°C

General description

Peptide-N-glycosidase F (PNGase F) belongs to an enzyme family, that are mainly used for the deglycosylation of N-linked glycans.

Application

PNGase Fast may be used to immobilize in order to perform deglycosylation. It may also be used to immobilize onto methacrylate based monolithic support to release the N-linked carbohydrate moieties from glycoproteins.

Biochem/physiol Actions

Peptide-N-glycosidase F (PNGase F) cleaves asparagine-linked high mannose, hybrid and complex oligosaccharides from glycoproteins. It can also deaminate the asparagine to aspartic acid. PNGase Fast enables complete and rapid deglycosylation of antibodies and immunoglobulin fusion proteins, as well as other glycoproteins, to be prepared for downstream chromatography or mass spectrometry analysis. PNGase Fast creates an optimized workflow, reducing processing time without compromising sensitivity or reproducibility.

WGK

WGK 3

Regulatory Information

常规特殊物品

Certificates of Analysis (COA)

Search for Certificates of Analysis (COA) by entering the products Lot/Batch Number. Lot and Batch Numbers can be found on a product’s label following the words ‘Lot’ or ‘Batch’.

Already Own This Product?

Find documentation for the products that you have recently purchased in the Document Library.

Visit the Document Library

David A Fischler et al.
Journal of biomolecular techniques : JBT, 30(4), 58-63 (2019-10-11)
There are several methods, both chemical and enzymatic, to release N-linked glycans for structural characterization. One of the most common enzymatic release methods is the use of peptide:N-glycosidase F (PNGase F). A less expensive and quicker alternative has been reported
Jana Krenkova et al.
Journal of chromatography. A, 1216(15), 3252-3259 (2009-03-10)
A reactor with immobilized peptide-N-glycosidase F on a monolithic polymer support in a capillary has been developed that allows fast and efficient release of N-linked glycans from immunoglobulin G molecules. Two different monolithic scaffolds based on poly(glycidyl methacrylate-co-ethylene dimethacrylate) and
Jamshid Khoshnoodi et al.
Journal of mass spectrometry : JMS, 42(3), 370-379 (2007-01-11)
Nephrin is a type-1 transmembrane glycoprotein and the first identified principal component of the glomerular filtration barrier. Ten potential asparagine (N)-linked glycosylation sites have been predicted within the ectodomain of nephrin. However, it is not known which of these potential
N-linked Glycan Release Efficiency: A Quantitative Comparison between NaOCl and PNGase F Release Protocols
Fischler DA and Orlando R
Journal of biomolecular techniques : JBT, 30, 58-58 (2019)
Oriented immobilization of peptide-N-glycosidase F on a monolithic support for glycosylation analysis
Krenkova J, et al.
Journal of Chromatography A, 1322, 54-61 (2013)

Articles

Fast assessment of antibody-dependent cell-mediated cytotoxicity (ADCC) and glycoform pattern of a therapeutic antibody rituximab by FcγRIIIa affinity chromatography.

Find deglycosylation kits for your research. Review the different features of deglycosylation kits for glycoproteins, enzymatic proteins, and native proteins.

PNGase Fast denaturing buffer and enzyme provide results similar to a conventional 20-hour protocol, reducing workflow time to about 1 hour.

Workflows for monoclonal antibody adalimumab characterization ensure drug safety and efficacy through critical quality attribute analysis.

See All

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