soluble protein expression in E. coli

ijiwaru at wheel.dcn.davis.ca.us ijiwaru at wheel.dcn.davis.ca.us
Tue Jan 16 13:39:03 EST 1996


In article <4dgton$iud at lyra.csx.cam.ac.uk>, sb at mole.bio.cam.ac.uk (Saverio
Brogna (Genetics)) wrote:

> Dear someone,
> I have expressed e protein in E. coli with differents systems (His-tag, 
> Glutation-transferase fusion and wild-type) but I can not get it soluble.
> DO YOU KNOW HOW TO EXPRESS PROTEINS IN A WAY THAT SOME IS SOLUBLE?
> 
> Thanks
> -- 
> Saverio Brogna
> University of Cambridge, Departement of Genetics
> Downing Street, Cambridge, CB2 3EH, England (UK)
> tel +44-223-333970, fax +44-223-333992

Invitrogen touts their thioredoxin fusion protein expression system as the
method of choice for proteins or protein domains with solubility
problems.  A person I work with is trying the system out now, but no
results to report.  You might try giving that one a try.  They claim that
you can heat the bacteria to precipitate out many of the bacterial
proteins and that the thioredoxin fusion partner will keep the protein of
interest in solution as a method to partially purify your protein.  You
might check out their web site (sorry, don't have the address on hand).

Lyle Najita
Plant Pathology
University of California - Davis

ps - no I don't get paid by Invitrogen.



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