Complex-type N-Linked Oligosaccharides

Most of our N-linked oligosaccharides are isolated from proteins from cell culture supernatants of CHO cells or BHK cells. These structures have core ?1-6 fucose and ?2-3-linked NeuAc and are available with and without N-acetyllactosamine repeats. They are used by our customers as reference standards in Quality Control release testing of pharmaceutical glycoproteins by glycosylation mapping procedures (HPAEC-PAD, mass spectrometry and others).

The underlying fully sialylated structures are analyzed by NMR, ESI-MS and MALDI/TOF-MS and are quantified by using two validated HPAEC-PAD based methods.
 

Di-antennary series of N-linked oligosaccharides

Diantennary N-glycans are present in many recombinant glycoprotein therapeutics and those from Chinese hamster ovary cells have exclusively ?2?3 linked NeuAc. TheraProteins also offers more than 35 N-glycan structures that are related to these glycans (truncated forms e.g. lacking Gal, Fuc, Gal1-4GlcNAc, monoantennary structures etc, and also glycans with different peripheral substitutions that are frequently encountered in recombinant products from CHO cells; see recombinant antibody N-glycan mapping).  Most of the diantennary glycans are also available with ?2?6 linked NeuAc and are fisolated rom natural human or other glycoproteins.

Phosphorylated oligomannosidic  (Man₅GlcNAc₂ / Man₆GlcNAc₂) and phosphorylated hybrid-type N-linked structures 

Phosphorylated  oligomannosidic or hybrid-type oligosaccharides present in recombinant therapeutic glycoproteins  ( CHO, BHK and HEK cells) may target the drug to undesired cells or tissues when applied in patients. In order to avoid these risks, cells culture supernatant as well as drug substance should be controlled for the absence of these oligosaccharides. TheraProteins is world wide the only company that offers a panel of these type of structures valuable in N-glycosylation mapping analysis of biopharmaceutical proteins at any stage of development.

Oligomannosidic N-glycans (Man₃GlcNAc₂ -  Man₉GlcNAc₂)

Incomplete/immature oligosaccharide chains and oligomannosidic N-glycans in biopharmaceutical glycoproteins should be avoided according to current opinion of regulatory authorities. If present in cell culture, the glycoforms containing these carbohydrate chains can be removed during appropriate down-stream processing steps or by medium / process optimization. TheraProteins oligomannosidic structures are used as reference standards in product optimization studies/development and also in quality testing.

Gal?1-3Galß1-4GlcNAc – motif containing N-linked structures

Some recombinant glycoproteins (e.g. from CHO cells) contain significant amounts of undesired glycan structures with the Gal?1-3Galß1-4GlcNAc–motif which are assumed to be antigenic in humans. TheraProteins provides appropriate reference oligosaccharides for detection of these glycans at early stages of biotech process set-up with mammalian expression systems and to quantitate them during downstream processing steps and in the final drug substance.

Lewis X and Sialyl Lewis X motif containing N-glycans

Oligosaccharide library for recombinant antibody N-glycan mapping

(More than 35 different structures)

For recombinant antibody glycosylation Quality Control release testing by oligosaccharide mapping/profiling procedures TheraProteins offers more than 35 different pure and fully characterized and quantified N-glycan structures that can be present in recombinant antibodies from e.g. CHO cells). Theraprotein´s sialylated glycan antibody library contains structures with NeuAc in ?2?3 linkage and all of them are available with and without proximal fucose. These structures are not supplied by other companies.
      In addition we also provide the structures with ?2?6 linked sialic acid containing oligosaccharides are also contained in our catalogue. 

 Not all of our structures are contained in the catalogue, please contact us in case you do not find  what you are looking for.