PNGase F Enzyme
Conditions of optimal PNGase F Enzyme performance should be determined experimentally by the investigator.
PNGase F from Elizabethkingia miricola (or Flavobacterium meningosepticum) catalyzes the cleavage of N-linked glycans from glycoproteins and glyopeptides. PNGase F has been widely used in combination with other glycosidases for proteomic and biochemical analysis. Various masss spectrometry methods, such as MALDI-TOF, and in vitro biochemical assays following deglycosylation catalyzed by PNGase F are used to identify the presence of N-linked oligosaccharides on glycoproteins and glyopeptides, and to analyze their importance for structure and function of glycoproteins and glyopeptides.
1. Mann, A.C., Self, C.H., and Turner, G.A. (1994) A general method for the complete deglycosylation of a wide variety of serum glycoproteins using peptide-N-glycosidase-F. Glycoconjugate Journal 1, 253–61.
BP004089-GD29: Recombinant PNGase F Enzyme (glycerol free)
Predicted molecular mass: 36 kDa
Unit Definition: One unit of the PNGase F enzyme catalyzes the release of >95% N-linked glycan from 10 ug of denatured RNase B in 10 ul at pH 7.5 in 1 hour at 37°C. One Syd Labs unit of PNGase F activity is equal to 0.015 IUB milliunit.
Formulation: The PNGase F solution (1,800 unit/ug) contains 50 mM Nacl, 5 mM EDTA, and 20 mM Tris-HCl, pH7.5 at 25°C.
Concentration: 500 unit/ul.
Purity: > 95% by SDS-PAGE and SEC-HPLC.
Shipping: The product is shipped with ice packs. Upon receipt, store it immediately at the temperature recommended below.
Stability & Storage:
Use a manual defrost freezer and avoid repeated freeze-thaw cycles.
12 months from date of receipt, 2 to 8°C as supplied.