Hello. We are going to use the 5 Prime cell-free expression system in our lab, to obtain a recombinant peptide of around 5 kDa. In most references is mentioned that the expression is successful only for proteins over 10 kDa. Does anyone has experience obtaining proteins with this system below this MW? Thanks in advance
Hi Amanda!
Just wondering - were you able to produce the peptide using your cell-free protein expression system? :-)
I haven't start it yet. The problem with chemical synthesis is that is difficult to achieve all 3 disulfide bond formation, same with E. coli. Im just considering some ideas...
Hello Amanda Vazquez , if you're still interested in the topic, I would suggest to go with the fusion of your target peptide with GST, its will help to increase the Mw of target peptide. Also this could help with ox/redox conditions (with GSH/GSSG buffer instead of DTT) for further formation of disulfide bonds.
- Badges
- Science method
- Similar topics
- Biological Science
- Genetics
- Gene Expression
- Protein Expression