≥20,000 units/mg protein
≥4500 units/mL for sensitive chromatographic and analytical workflows requiring minimal baseline interference.
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Storage & shipping
Store at 2-8°C Ships Wet ice Check lot-specific COA for exact specifications.
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Quality documents
SDS, COA, datasheet, and spec sheet available for download. Lot-specific COA accessible via lot number lookup.
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Literature proof
Cited in 0 peer-reviewed publications across chromatography, organic synthesis, and cross-coupling reactions.
Overview
Native N-Glycosidase F from Elizabethkingia meningosepticum. Catalyzes the hydrolysis of asparagine-linked high mannose, as well as hybrid and complex oligosaccharides from glycoproteins. This enzyme will not cleave oligosaccharides containing α1,3-linked core fucose commonly found on plant glycoproteins. N-Glycosidase F will also fail to cleave if the asparagine to which the oligosaccharide is attached is not peptide-bonded to at least one amino acid residue at both the amino and carboxy termini.
Native N-Glycosidase F from Elizabethkingia meningosepticum. Catalyzes the hydrolysis of asparagine-linked high mannose, as well as hybrid and complex oligosaccharides from glycoproteins. This enzyme will not cleave oligosaccharides containing α1-3-linked core fucose commonly found on plant glycoproteins. N-Glycosidase F will also fail to cleave if the asparagine to which the oligosaccharide is attached is not peptide-bonded to at least one amino acid residue at both the amino and carboxy termini.
Specifications
Product Name
N-Glycosidase F, Elizabethkingia meningosepticum
Specifications & Purity
≥20, 000 units/mg protein
≥4500 units/mL
Molecule Type
Enzyme
Storage and Shipping
Concentration
≥20,000 units/mg protein
≥4500 units/mL
Storage
Store at 2-8°C
Shipped In
Wet ice
Documentation
📋 Safety Data Sheet (SDS)
Comprehensive hazard, handling, storage, and regulatory compliance document.
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