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Yes, the transglycosylation reaction can be performed on all subclasses of human IgG. The reaction is somewhat slower on IgG2 and longer incubation times may be necessary to obtain over 95% transglycosylation.

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Unfortunately no, the enzyme requires trimming of the Fc-glycan using GlycINATOR to enable access to the core fucose substrate.

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The TransGLYCIT platform is developed for transglycosylation of human IgG.

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GlycINATOR is an IgG specific endoglycosidase that hydrolyzes complex, hybrid and high mannonse type glycans on the conserved Fc site on IgG.

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No, TransGLYCIT is based on IgG specific enzymes and will only transglycosylate IgG.

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The recommended buffer for best performance of the column is TBS buffer at pH 8.6. Other buffers with neutral pH containing 0.15 M NaCl can also be used but optimization may then be required.

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The columns are recommended to be used for deglycosylation at native conditions only.

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No, it is not recommended. We can only guarantee optimal performance for one-time use.

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PNGase F Immobilized hydrolyzes the amide bond between the polypeptide asparagine and the innermost GlcNAc of all mammalian asparagine-linked complex, hybrid, or high mannose oligosaccharides. It does not remove N-glycans with α1-3 core fucosylation.

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Yes! Contact us at info@genovis.com

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