“Ecobody” is a technology developed at Nagoya University, Japan, enabling us to obtain and evaluate useful antibodies produced in humans and animals exhaustively and rapidly.
Benefits of “Ecobody” Technology
With “Ecobody” technology, we can obtain monoclonal antibodies individually from single human and animal B cells.
Unlike conventional technology, our technology does not require immortalization or proliferation of B cells, avoiding cell loss. Therefore, we can mine monoclonal antibodies while maintaining the original diversity seen in humans and animals.
In addition, while conventional antibody expression systems use living cells that cause heterogeneity in expression levels, “Ecobody” technology uses a cell-free system to express antibodies, resulting in homogeneous antibody levels.
Our technology contributed to the exhaustive and rapid (2 days) evaluation of antibodies without decreased diversity.
Please see the video below and references for technical details.
・Tagged antibody（Japan Patent No. 6744670）
・Protein Expression Method（Japan Patent No. 6681625; U.S. Patent Number: 10975376）
※iBody has been granted an exclusive global license for these patents from Nagoya University.
Features of Antibody Mining Technologies
|Animals||Rabbit, Human||Mouse||Not used|
|Time||2 days※||A few months||7 weeks|
|Core Technology||Single-cell technology and in vitro antibody expression||Cell fusion and culture||Bacterial expression|
|Native Antibody Isolation||Possible||Possible||Impossible|
※Excludes the animal immunization period
- Rapid Generation of Monoclonal Antibodies from Single B Cells by Ecobody Technology. Antibodies, 7, 38 (2018)
- Ecobody technology: rapid monoclonal antibody screening method from single B cells using cell-free protein synthesis for antigen-binding fragment formation. Sci Rep, 7, 13979 (2017)
- N-terminal SKIK peptide tag markedly improves expression of difficult-to-express proteins in Escherichia coli and Saccharomyces cerevisiae. J Biosci Bioeng. 123, 540 (2017)
- ‘Zipbody’ leucine zipper-fused Fab in E. coli in vitro and in vivo expression systems. Protein Eng Des Sel. 29, 149 (2016)