Endoglycosidase F1 (Endo F1) from Elizabethkingia miricola, is an enzyme used for removing N-linked oligosaccharides from glycoproteins.
Endoglycosidase F1, expressed in E. coli, cleaves asparagine linked or free high mannose (oligomannose) and hybrid structures. It differs from exoglycosidase, that is does not do so at the terminal residue. This enzyme is suitable for deglycoslylation of N-linked oligosaccharides from glycoproteins under native conditions, and is appropriate for a variety of glycomics, proteomics, and mass spectroscopy applications.
From the laboratory of Davide Comoletti, DVM, PhD, Rutgers University
Part of The Investigator's Annexe program.
|Name:||Endoglycosidase F1 (endo F)|
|Accession ID:||Uniprot P36911|
|Molecular Weight:||63 kDa (with the Tag)|
|Buffer:||20 mM TRIS pH 8.0, 150 mM NaCl, 1 mM DTT, 20 % Glycerol|
|Comments:||Plasmid pGEX 3X, Expressed in E. coli BL21 (DE3)|
For efficient deglycosylation, use overnight incubation (~16 h) at 4 deg C with a ratio 1:20 (ug enzyme:ug target protein), in mid pH conditions (Suggested; 50 mM TRIS pH 7.5, 150 mM NaCl).
SDS-PAGE analysis showing purification of PNGase F on the left, Ladder in the middle, and Endo F1 on the right.
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