Production of bioactive trastuzumab and chimeric anti-VEGF antibody in the cytoplasm of Escherichia coli

Conference proceedings article

ผู้เขียน/บรรณาธิการ

อัศวิน มีชัย

กลุ่มสาขาการวิจัยเชิงกลยุทธ์

ไม่พบข้อมูลที่เกี่ยวข้อง

รายละเอียดสำหรับงานพิมพ์

รายชื่อผู้แต่ง: Charoenpun P., Leelawattanachai J., Meechai A., Waraho-Zhmayev D.

ผู้เผยแพร่: IOP Publishing

ปีที่เผยแพร่ (ค.ศ.): 2018

Volume number: 185

Issue number: 1

นอก: 1755-1307

eISSN: 1755-1315

URL: https://www.scopus.com/inward/record.uri?eid=2-s2.0-85053779606&doi=10.1088%2f1755-1315%2f185%2f1%2f012003&partnerID=40&md5=cbf8d9bfd0c6584a5a0cfafd95690c0b

ภาษา: English-Great Britain (EN-GB)

ดูในเว็บของวิทยาศาสตร์ | ดูบนเว็บไซต์ของสำนักพิมพ์ | บทความในเว็บของวิทยาศาสตร์

บทคัดย่อ

Monoclonal antibody (mAb) is a very useful tool in not only medical field but also in research field. However, the current cost of its production is very high as most mAbs are produced in mammalian cell system. Escherichia coli is a good alternative but has many bottlenecks. Recently, it was demonstrated that biological active full-length Immunoglobulin G (IgG) could be produced in the reductive cytoplasm of an engineered E. coli strain called SHuffle. In this study, we investigated the effect of temperature and induction level on the production of full-length humanized anti-Her2 and chimeric anti-VEGF IgGs expressed as cyclonal. The solubility as well as the assembly of the IgG molecules was examined by western blot analysis. It was found that expression at 30 ฐC with 0.1 mM IPTG induction was the most suitable for trastuzumab. In contrast, the full-length expression of chimeric anti-VEGF required induction with 1 mM IPTG at 30 ฐC., however, 1 mM IPTG induction resulted in more full-length IgG. In conclusion, the present study indicated that E coli could be successfully used for the full-length expression of IgG by suitably modifying the expression conditions. ฉ 2018 Institute of Physics Publishing. All rights reserved.

คำสำคัญ