Fusion with CTP increases the stability of recombinant neuritin.
In: Protein expression and purification, Jg. 212 (2023-12-01), S. 106344
academicJournal
Zugriff:
Neuritin is a vital neurotrophin that plays an essential role in recovery from nerve injury and neurodegenerative diseases and may become a new target for treating these conditions. However, improving neuritin protein stability is an urgent problem. In this study, to obtain active and stable neuritin proteins, we added a carboxyl-terminal peptide (CTP) sequence containing four O-linked glycosylation sites to the C-terminus of neuritin and cloned it into the Chinese hamster ovary (CHO) expression system. The neuritin-CTP protein was purified using a His-Tag purification strategy after G418 screening of stable high-expression cell lines. Ultimately, we obtained neuritin-CTP protein with a purity >90%. Functional analyses showed that the purified neuritin-CTP protein promoted the neurite outgrowth of PC12 cells, and stability experiments showed that neuritin stability was increased by adding CTP. These results indicate that neuritin protein-CTP fusion effectively increases stability without affecting secretion and activity. This study offers a sound strategy for improving the stability of neuritin protein and provides material conditions for further study of the function of neuritin.
(Copyright © 2023 Elsevier Inc. All rights reserved.)
Titel: |
Fusion with CTP increases the stability of recombinant neuritin.
|
---|---|
Autor/in / Beteiligte Person: | Meng, P ; Wei, Y ; Liang, M ; Yuan, W ; Zhu, L ; Sun, J ; Huang, J ; Zhu, J |
Zeitschrift: | Protein expression and purification, Jg. 212 (2023-12-01), S. 106344 |
Veröffentlichung: | Orlando, FL : Academic Press ; <i>Original Publication</i>: San Diego : Academic Press, c1990-, 2023 |
Medientyp: | academicJournal |
ISSN: | 1096-0279 (electronic) |
DOI: | 10.1016/j.pep.2023.106344 |
Schlagwort: |
|
Sonstiges: |
|