hi 

In the post-genomic era, the need for highly purified recombinant protein for biophysical and biochemical studies is greater than ever. In this regard, the laboratory workhorse, Escherichia coli, has been essential for the simple low-cost expression of the majority of proteins investigated to date. However, a number of biomedically relevant proteins fail to express and fold properly in prokaryotic expression hosts. For example, mammalian secreted proteins and membrane bound receptors often contain obligate post-translational modifications including disulfide bonds and unique glycosylation patterns that are required for proper folding and/or biological activity, preventing their expression in prokaryotes. Alternatively, a number of powerful eukaryotic expression systems are available for expression of challenging proteins including those that contain unique post-translational modifications. The most common over-expression platforms currently include yeast (e.g., Pichia pastoris and Saccharomyces cerevisiae), baculovirus expression vector systems (Autographa californica multiple nuclear polyhedrosis virus and insect cell hosts Spodoptera frugiperda or Trichoplusia ni), and mammalian cell systems (including a variety of transformed cell lines such as CHO and HEK293). It should be noted that each expression platform has its own merits and disadvantages, and one may be more suitable for a particular protein over others.

Hi,

I read that paper before but it doesnt seem to provide any numbers! Sorry!