by Thierry Battle, PhD et al.
Volume 6, Issue 4 (Winter 2007)
In order to unravel new protein activities and functions, we have expressed and purified a large number of human proteins. We have chosen to study secreted proteins and the extra-cellular domains of putative single transmembrane domain-containing proteins. In order to retain the natural protein characteristics as far as possible, we have used a mammalian expression system. Human embryonic kidney (HEK293) cells were chosen as they have been shown to possess a high protein-secretory potential. The secreted proteins were expressed with a carboxy-terminal tag and purified by affinity chromatography. Each protein was produced at a routine scale from 500 ml cell cultures, and the secreted protein was purified from the culture supernatant…
Citation:
Battle T et al. Transient HEK293 Recombinant Protein Production Flow: The Replenishment of Protein Batches By Outsourcing to a Contract Research Organization. BioProcess J, 2007; 6(4): 31-38. http://dx.doi.org/10.12665/J64.Battle