Versatile Expression System for Rapid and Stable Production of Recombinant Proteins
- 1 January 2003
- journal article
- research article
- Published by Wiley in Biotechnology Progress
- Vol. 19 (1) , 229-232
- https://doi.org/10.1021/bp0255964
Abstract
Previously we reported the development of a novel expression system with Tat/TAR‐oriP vectors and HKB11 cell line, which supports high level protein expression (Cho et al. Cytotechnology 2001, 37, 23–30). In the present study, we further demonstrated that HKB11 cells are suitable for high throughput expression (microgram scale) of genomic candidates in transient transfection system for in vitro evaluation of biological functions. HKB11 cells were also shown to support the production of milligram to gram quantities of protein drug candidates for in vivo evaluation of efficacy in various disease models. Stable HKB11 clones secreting high levels of a tissue factor (TF; 40–50 pg/c/d) and B‐domain deleted recombinant factor VIII (BDDrFVIII; 5–10 μU/c/d) were derived under serum‐free conditions. The specific productivity for these two proteins from the HKB11 cells was 10‐fold greater than those from CHO cells derived under the similar conditions. In conclusion, we have demonstrated that the HKB11 cell line is well‐suited for transient and long‐term production of recombinant proteins.Keywords
This publication has 12 references indexed in Scilit:
- Establishment of a human somatic hybrid cell line for recombinant protein productionJournal of Biomedical Science, 2002
- Recombinant protein expression for therapeutic applicationsCurrent Opinion in Biotechnology, 2002
- High-level and high-throughput recombinant protein production by transient transfection of suspension-growing human 293-EBNA1 cellsNucleic Acids Research, 2002
- Industrial choices for protein production by large-scale cell cultureCurrent Opinion in Biotechnology, 2001
- Therapeutic antibody expression technologyCurrent Opinion in Biotechnology, 2001
- An oriP expression vector containing the HIV-1 Tat/TAR transactivation axis produces high levels of protein expression in mammalian cellsCytotechnology, 2001
- Tat trans-activates the human immunodeficiency virus through a nascent RNA targetCell, 1989
- Construction and characterization of an active factor VIII variant lacking the central one-third of the moleculeBiochemistry, 1986
- A cis-acting element from the Epstein-Barr viral genome that permits stable replication of recombinant plasmids in latently infected cells.Proceedings of the National Academy of Sciences, 1984
- Isolation of Chinese hamster cell mutants deficient in dihydrofolate reductase activity.Proceedings of the National Academy of Sciences, 1980