Dirk,
Your question is not clear. Are you saying that the natural form of this
protein is known to be a tetramer but your recombinant material is
monomeric? If this is true then I would have to say that your
recombinant form is most likely not properly folded. How was it
expressed and purified? Also, how sure are you about your information
regarding the quaternary structure of the natural and recombinant
material (such assignments can be wrong, especially if based on
size-exclusion chromatography)? Do you have natural material for
side-by-side comparisons?
John Philo
Alliance Protein Laboratories
www.ap-lab.com
Dirk Seegert wrote:
>> Hi there,
> I wonder wheather anybody could give me hints on how to get a monomeric
> recombinant protein into its natural occuring bioactive tetrameric form. Is
> it possible to solve this problem by production of tagged proteins? If so,
> which tags could be useful? Do I have to use specific cell lines?
> I would be happy for any advice.
>> Thanx,
> Dirk Seegert
>> ****************************************
> Dr. Dirk Seegert
> Christian-Albrechts-Universität Kiel
> 1. Medizinische Klinik, Mucosaimmunologie
> Schittenhelmstr. 12
> D-24105 Kiel
> GERMANY
>> Tel. +49 (431) 597-1373
> Fax +49 (431) 597-1842
>http://www.mucosa.de>> ---
