protein

PNGase F Protein, F. meningosepticum (His)

HY-P79356

5 μg;10 μg;50 μg

62;105;294 USD

PNGase F Protein, F. meningosepticum (His)

proteins

E. coli

5 μg;10 μg;50 μg

62;105;294 USD

The PNGase F protein acts as an enzyme catalyst that specifically cleaves entire glycans from glycoproteins. This process depends on the replacement of the glycosylated asparagine moiety by a polypeptide chain at both its amino (R1) and carboxyl (R2) termini, as shown in Reaction 1. PNGase F Protein, F. meningosepticum (His) is the recombinant PNGase F protein, expressed by E. coli , with N-His labeled tag. The total length of PNGase F Protein, F. meningosepticum (His) is 314 a.a., with molecular weight of ~35 kDa.

Others

PNGase F (Peptide:N-glycosidase F) is a protein with the remarkable ability to cleave an entire glycan from a glycoprotein. This enzymatic process involves the removal of the glycosylated asparagine moiety, specifically requiring that the asparagine be substituted on both its amino (R1) and carboxyl (R2) termini with a polypeptide chain. PNGase F plays a pivotal role in the analysis and manipulation of glycoproteins by facilitating the release of N-linked glycans. This enzymatic activity is crucial for various applications in the study of protein glycosylation, allowing researchers to investigate the structural and functional implications of glycan modifications on proteins (

PNGase F; PNGF; Peptide-N4-(N-acetyl-beta-D-glucosaminyl)asparagine Amidase F

Greater than 95% as determined by reducing SDS-PAGE

Supplied as a 0.2 μm filtered solution of PBS, pH 7.4, 10% Glycerol.

Shipping with dry ice