P0709S,  PNGase F (Glycerol Free), recombinant - 15.000 units

P0709S, PNGase F (Glycerol Free), recombinant - 15.000 units

P0711S,  Rapid PNGase F (non-reducing format) - 50 reactions

P0711S, Rapid PNGase F (non-reducing format) - 50 reactions

P0710S, Rapid PNGase F - 50 reactions

3.416,49 RON

Rapid PNGase F enables complete and rapid deglycosylation of antibodies and immunoglobulin fusion proteins, as well as other glycoproteins, in minutes. All N-glycans are released rapidly and without bias, and are ready to be prepared for downstream chromatography or mass spectrometry analysis. Rapid PNGase F creates an optimized workflow, reducing processing time without compromising sensitivity or reproducibility.

SKU
NEB_P0710S

Deglycosylation in minutes for N-glycan analysis

Rapid PNGase F enables complete and rapid deglycosylation of antibodies and immunoglobulin fusion proteins, as well as other glycoproteins, in minutes. All N-glycans are released rapidly and without bias, and are ready to be prepared for downstream chromatography or mass spectrometry analysis. Rapid PNGase F creates an optimized workflow, reducing processing time without compromising sensitivity or reproducibility.

  • Complete deglycosylation of antibodies and immunoglobulin fusion proteins in 10 minutes
  • Recombinant enzyme; guaranteed endoglycosidase F1, F2 or F3 free
  • All reaction components are compatible with HPLC and mass spectrometry analysis
  • ≥ 95% purity, as determined by SDS-PAGE and intact ESI-MS
  • Optimal activity and stability ensured for up to 12 months
  • Fast reaction setup

 

Application Features

Rapid PNGase F is an improved recombinant reagent that allows the complete and rapid deglycosylation of antibodies and fusion proteins in only minutes. All N-glycans are released rapidly and without bias, ready to be prepared for downstream chromatography or mass spectrometry analysis.

A variety of therapeutic monoclonal antibodies were used to validate Rapid PNGase F: different subclasses (IgG 1 to 4), isotypes (IgA, IgM, IgE), organisms (mouse, human, and humanized), sources (CHO, murine myeloma), and structures (IgG, IgG-fusions).

Rapid PNGase F can effectively remove all N-glycans from both conserved (i.e. Fc Asn297) and non-conserved (i.e. Fab N-glycans) glycosylation sites. Validation was in accordance with published data. Sensitivity and specificity are not compromised by a faster and more convenient glycoprotein characterization workflow using Rapid PNGase F.

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Price 2.871,00 RON (preturile sunt fara TVA)
Description

Deglycosylation in minutes for N-glycan analysis

Rapid PNGase F enables complete and rapid deglycosylation of antibodies and immunoglobulin fusion proteins, as well as other glycoproteins, in minutes. All N-glycans are released rapidly and without bias, and are ready to be prepared for downstream chromatography or mass spectrometry analysis. Rapid PNGase F creates an optimized workflow, reducing processing time without compromising sensitivity or reproducibility.

  • Complete deglycosylation of antibodies and immunoglobulin fusion proteins in 10 minutes
  • Recombinant enzyme; guaranteed endoglycosidase F1, F2 or F3 free
  • All reaction components are compatible with HPLC and mass spectrometry analysis
  • ≥ 95% purity, as determined by SDS-PAGE and intact ESI-MS
  • Optimal activity and stability ensured for up to 12 months
  • Fast reaction setup

 

Application Features

Rapid PNGase F is an improved recombinant reagent that allows the complete and rapid deglycosylation of antibodies and fusion proteins in only minutes. All N-glycans are released rapidly and without bias, ready to be prepared for downstream chromatography or mass spectrometry analysis.

A variety of therapeutic monoclonal antibodies were used to validate Rapid PNGase F: different subclasses (IgG 1 to 4), isotypes (IgA, IgM, IgE), organisms (mouse, human, and humanized), sources (CHO, murine myeloma), and structures (IgG, IgG-fusions).

Rapid PNGase F can effectively remove all N-glycans from both conserved (i.e. Fc Asn297) and non-conserved (i.e. Fab N-glycans) glycosylation sites. Validation was in accordance with published data. Sensitivity and specificity are not compromised by a faster and more convenient glycoprotein characterization workflow using Rapid PNGase F.