The binding of fully human monoclonal antibodies (MAbs) D2E7 and 2SD4 to their antigen, human tumor necrosis factor-alpha (TNFalpha), was investigated by BIAcore, cation exchange (CIEX), and size exclusion liquid chromatography (SEC) using ultraviolet and laser light scattering detectors. D2E7 has a
Characterization of the glycosylation state of a recombinant monoclonal antibody using weak cation exchange chromatography and mass spectrometry
โ Scribed by Georgeen Gaza-Bulseco; Ashley Bulseco; Chris Chumsae; Hongcheng Liu
- Book ID
- 108159814
- Publisher
- Elsevier Science
- Year
- 2008
- Tongue
- English
- Weight
- 670 KB
- Volume
- 862
- Category
- Article
- ISSN
- 1873-376X
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Cation-exchange liquid chromatography (CIEX) and capillary isoelectric focusing (cIEF) methods have been developed for the routine analysis of a recombinant, human anti-tumor necrosis factor monoclonal antibody D2E7. Both of these methods can separate heavy-chain C-terminal variants of this antibody
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