P0706S,  Remove-iT PNGase F - 6.750 units

P0706S, Remove-iT PNGase F - 6.750 units

P0707S,  PNGase A - 150 units

P0707S, PNGase A - 150 units

P0707L, PNGase A - 750 units

8.056,90 RON

PNGase A cleaves between the innermost GlcNAc and asparagine residues of high mannose, hybrid, and short complex oligosaccharides such as those found in plant and insect cells from N-linked glycoproteins and glycopeptides. PNGase A differs from PNGase F in that it cleaves N-linked glycans with or without α(1,3)-linked core fucose residues.

SKU
NEB_P0707L

PNGase A cleaves between the innermost GlcNAc and asparagine residues of high mannose, hybrid, and short complex oligosaccharides such as those found in plant and insect cells from N-linked glycoproteins and glycopeptides. PNGase A differs from PNGase F in that it cleaves N-linked glycans with or without α(1,3)-linked core fucose residues.

  • Cleaves N-glycans from plant and insect derived glycoproteins and glycopeptides
  • Activity is not inhibited by an α1-3 Fucose residue on the chitobiose core
  • Recombinant enzyme with no detectable exoglycosidase or other endoglycosidase contaminating activities
  • Glycerol-free for optimal performance in HPLC and mass spectrometry analysis
  • ≥95% purity, as determined by SDS-PAGE and intact ESI-MS
  • Optimal activity and stability for up to 24 months 

 

Product Source

Cloned from Oryza sativa (rice) and expressed in Pichia pastoris.

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Price 6.770,50 RON (preturile sunt fara TVA)
Description

PNGase A cleaves between the innermost GlcNAc and asparagine residues of high mannose, hybrid, and short complex oligosaccharides such as those found in plant and insect cells from N-linked glycoproteins and glycopeptides. PNGase A differs from PNGase F in that it cleaves N-linked glycans with or without α(1,3)-linked core fucose residues.

  • Cleaves N-glycans from plant and insect derived glycoproteins and glycopeptides
  • Activity is not inhibited by an α1-3 Fucose residue on the chitobiose core
  • Recombinant enzyme with no detectable exoglycosidase or other endoglycosidase contaminating activities
  • Glycerol-free for optimal performance in HPLC and mass spectrometry analysis
  • ≥95% purity, as determined by SDS-PAGE and intact ESI-MS
  • Optimal activity and stability for up to 24 months 

 

Product Source

Cloned from Oryza sativa (rice) and expressed in Pichia pastoris.