Elizabethkingia meningoseptica Recombinant N-Glycanase (PNGase F) (from E. coli)
Supplier: AGILENT TECHNOLOGIES, INC (CSD)
Enzyme releases intact N-glycans by cleaving between the innermost GlcNAc and Asn. A recombinant form of PNGase F, 200mU, 1mMEDTA. GKE-5010D pack size does not ship with reaction buffers, however reaction buffers are available on request.
- pH range: 7.5-9.5 (Optimum: 8.6)
- Unit definition: One unit is defined as the amount of enzyme required to catalyze the release of N-linked oligosaccharides from 1 µmole of denatured ribonuclease B per minute at pH 7.5 and 37°C.
To obtain efficient deglycosylation of glycoprotein substrates under nondenaturing conditions, it is necessary to use a higher starting concentration of enzyme. N-Glycanase PLUS and ULTRA (EDTA-Free) are supplied at = 10 U/ml, and are recommended for all applications requiring deglycosylation of glycoproteins in the absence of denaturants. The high activity also allows smaller reaction volumes and shorter reaction times to be explored.
Source: Recombinant gene from Elizabethkingia meningoseptica, expressed in E. coli. The source organism was previously known as Chryseobacterium [Flavobacterium] meningosepticum. Enzyme also known as PNGase F, peptide-N-glycosidase F, peptide-N4-(N-acetyl-β-glucosaminyl)asparagine amidase.
Specifictiy: Cleaves all N-linked complex, hybrid or high mannose oligosaccharides, unless a(1-3) core fucosylated, as in plant glycans. Asparagine must be peptide bonded at both termini. Phosphate, sulfate, and sialic acid groups attached to the oligosaccharide do not affect cleavage. Endo F free. Highly concentrated, particularly useful for deglycosylation under native conditions.
Learn more
About VWR
Avantor is a vertically integrated, global supplier of discovery-to-delivery solutions for...