We believe this site might serve you best:

United States

English Continue

This country code will remain if no action is taken to change it.

Don't see your country?
Promega Corporation

PNGase F / Endo H

Glycosylation is protein modification that adds a carbohydrate group to specific amino acid residues of a protein. N-linked glycosylation is the most common type of glycosidic bond. PNGase F and Endo H are two specific endoglycosidases used to characterize glycoproteins.

Learn more about specific applications below.

Using Endo H and PNGase F to monitor protein trafficking

The unique specificity of Endo H and PNGase F can be used to monitor protein trafficking. Basic N-glycosylation occurs in the endoplasmic reticulum where proteins in this stage are sensitive to Endo H digestion. Proteins that have entered the Golgi body, where additional modifications occur to the glycan, and are resistant to Endo H digestion.

Learn More »

Figure 11003MA Click to Enlarge
/-/media/images/resources/figures/11000-11099/11003ma_700px.jpg

Gel analysis of glycoproteins treated with PNGase F

Determining whether a protein is in fact glycosylated is the initial step in glycoprotein analysis. SDS-PAGE has become the method of choice as the final step prior to mass spec analysis. A marked decrease in band width and change in migration position after treatment with PNGase F is considered evidence of N-linked glycosylation.

Learn More »

Figure 11186TB Click to Enlarge
/-/media/images/resources/figures/11100-11199/11186tb_680px.jpg

Analyze glycoproteins with LC-MS/MS and PNGase F

Gel-based data is often correlated with information obtained from mass spec analysis. Asn-linked type glycans can be cleaved enzymatically by PNGase F yielding intact oligosaccharides and a slightly modified protein in which Asn residues at the site of de-N-glycosylation are converted to Asp. The deglycosylated peptides are then analyzed by mass spectrometry.

Learn More »

1158MD330x258 Click to Enlarge
/-/media/images/resources/figures/11500-11599/1158md300x258.jpg

It appears that you have Javascript disabled. Our website requires Javascript to function correctly. For the best browsing experience, please enable Javascript.