Suppose you are trying to express a protein in Bacteria but that protein is coming in Inclusion bodies but not secreted out. So is it possible if I express that same protein in mammalian cell with signal peptide to make it secreted out in the supernent so that I can purify it easily ?
Is the protein originally from bacteria? You would need to add a poly A tail onto the transcript for the gene. As for the signal peptide there are many options (Article Enhancing heterologous protein expression and secretion in H...
).
Theoretically is possible,
Practically is it possible that you protein will be subjected to some PMT as glycosilation that are not present in bacteria and it is possible that this PMT may alter the protein functionality.
I'm a fun of mammalian expression sistem (in my blog ProteoCool you can find some post about EXpi293 and ExpiCHO that i found amazing) but probabily before move to mammalian, i will perform some more trial in bacteria (eg perfromin periplamic expression if the protein contain cisteines, or redesign the protein domain or add an N-terminal fusion tag)
good luck
Manuele
Sebastian Schmitt
sir I'd like to know what is the advantage of co expressing with an Interaction partner ?- Badges
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