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Specifications
- Enzyme type:Recombinant
- Source:E. coli
- Species:Flavobacterium meningosepticum
- Size:2×50 µl (100 µl total)
- Environmentally Preferable:
- Storage Conditions:Storage: –20 or 4 °C (avoid multiple freeze-thaws)
- Enzyme Name:PNGase F PRIME Glycosidase
- Concentration:1,000 units/ µl
- Cat. No.:102830-006
- Supplier no.:NZPP050
Specifications
About this item
PNGase F PRIME is a mutant recombinant PNGase F cloned from Flavobacterium meningosepticum and expressed and purified from E. coli. The proprietary changes made to PNGase F have been shown to have unique characteristics when compared to other commercially-available sources of PNGase F. Data generated by independent labs shows that PRIME works on native glycoproteins and serum glycoproteins in minutes at room temperature. Glycan analysis of the digestion products shows that PNGase F PRIME digestion led to more complete glycan release and also allowed for the cleavage of glycans not released by the commercially-available enzymes when used at the same concentrations with the same digestion conditions. This advancement benefits applications that seek to understand glycobiology in a natural milieu. Preliminary data indicates that PNGase F PRIME has a higher specificity towards complex (tri and tetra-antennary) sialylated structures compared to the commercially sourced enzyme. Additionally, the work presented in this Analytical Chemistry paper utilized PNGase F PRIME for all in situ tissue work as the commercially-available PNGase enzymes did not work on native tissue to allow glycan recognition.
- Great for native and denatured glycoproteins
- Contains NO glycerol
- Contains a His-tag
- Compatible with Mass Spec
- Specifically remove oligosaccharides from proteins
- Target: Asparagine-linked (N-linked) oligosaccharides (mannose, hybrid, and complex)
PNGase F PRIME-LY Glycosidase is the same enzyme as our standard PNGase F PRIME but now available in a lyophilized form, which is perfectly suitable for use in solution-based analyses. Performance characteristics and applications in which PNGase F PRIME-LY can be used remain exactly the same as with our standard liquid format PNGase F PRIME enzyme.
Excellent for use in high-end use applications especially those using or requiring UPLC/HPLC, Hydrophilic Interaction Chromatography (HILIC), and/or MALDI-Glycan Mass Spec Imaging.
Released glycans can be examined following labeling with the Waters RapiFluor-MS dye and analyzed by normal phase hydrophilic interaction chromatography (HILIC) using various HPLC/UPLC-based systems.
Imaging of released glycans directly on tissue can be done following spraying of enzyme on tissue and incubation at 37°C for 1 hour. (At our standard concentration of 2mg/mL, one 50 µL vial can make 4 slides.) Glycan can be detected using instruments such as the Bruker Daltonics SolariX™ 7T Hybrid FTMS System, a Bruker Daltonics RapifleXTM MALDI Tissuetyper, or a Bruker Daltonics UltrafleXtreme MALDI-TOF/TOF mass spectrometer."