soluble protein expression in E. coli

Robert Seymour r.seymour at prospect.anprod.csiro.au
Tue Jan 16 21:44:24 EST 1996


In article <4dgu30$j6a at lyra.csx.cam.ac.uk>,
   sb at mole.bio.cam.ac.uk (Saverio Brogna (Genetics)) wrote:
>Dear someone,
>
>I have expressed a Drosophila protein  in E. coli by using several 
>strategies (unfused, fused to glutation transferase, and fuse to 6-His 
>tag) but all of it is unsoluble.
>DO YOU KNOW OF ANY WAY TO EXPRESS PROTEINS IN E. COLI THAT ARE SOLUBLE?
>
>THANKS SAVERIO


Saverio 

Welcome to the club of people expressing eukaryotic proteins in E. coli that 
turn out to be insoluble.  There is some published literature around (though 
I can't remember any off the top of my head) that talk about the use of 
chaperones expressed in conjunction with insoluble eukaryotic proteins to 
improve their folding in E.coli and thus solubility.  These chaperones are 
called (I think)gro E and gro L and expression sytems that use them are 
available commercially (I think).

Robert

CSIRO Division of animal production
Prospect, NSW
Australia

(The usual disclaimer)



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