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PNGase F cleaves the β-aspartylglucosamine bond between the N-Acetylglucosamine (GlcNAc) and asparagine linkage

PNGase F

Item Id: FSB0002

Your Price:

$119.00

Price and Availability

Amount
	0.4 U [$119] 1.5 U [$419]

Quantity

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Description
Technical Information
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Recombinant PNGase F

Affinity purified, robust enzyme for N-linked glycan removal

Removal of N-linked glycans under denaturing or non-denaturing conditions. PNGase F, peptide N-glycosidase F, is a recombinantly expressed endoglycosidase from Flavobacterium meningosepticum that cleaves the β-aspartylglucosamine bond between the N-Acetylglucosamine (GlcNAc) and asparagine linkage of N-linked oligosaccharides in glycoproteins. This cleavage point acts as a convenient identification point in subsequent mass spectroscopy analysis.

Properties
Quantity	0.4 U
Specific Activity	>10 U/mg
Purity	>95% by SDS-PAGE
Molecular Weight	34,800 daltons (Apparent)
Extinction coefficient	1 mg/ml = 2.01/cm path length (Calculated) at 280 nm
Theoretical pI	8.39
Storage	Format: Liquid
	Buffer: 20 mM Tris - pH 7.5, 50 mM NaCl, 0.5 mM EDTA
	Temperature: 4°C.
	Stability: 1 year
Units	One unit is defined as the amount of enzyme required to catalyze the release of >95% N-linked oligosaccharides from 60 μmoles of denatured ribonuclease B in 1 hour at 37C, pH 7.5. One micromolar unit of PNGase F activity is equal to 1,000 nanomolar units (IUB milliunits).

Supplied Reagents

Enzyme (stored in 20 mM Tris - pH 7.5, 50 mM NaCl, 0.5 mM EDTA)
10X Deglycosylation Reaction Buffer (0.5 M sodium phosphate – pH 7.5)

Supporting Documents

Product Specification Sheet - lot 07C07

Product Specification Sheet - lot 031113

Material Safety Data Sheet