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An engineered human IgG1 CH2 domain with decreased aggregation and nonspecific binding
The immunoglobulin (Ig) CH2 domain is a promising scaffold for the development of candidate therapeutics. We have previously shown that the stability of isolated CH2 could be increased by the introduction of an additional disulfide bond and removal of seven N-terminal residues (m01s). However, both...
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| Main Authors: | , , , , , , |
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| Formato: | Artigo |
| Idioma: | Inglês |
| Publicado em: |
Taylor & Francis Group
2020-01-01
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| Colecção: | mAbs |
| Assuntos: | |
| Acesso em linha: | https://www.tandfonline.com/doi/10.1080/19420862.2019.1689027 |
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