Another option would be to use a protease immobilized in some resin (for
instance GST-tagged TEV protease bound to GSH-Agarose resin, in column or
in batch), so that no protease would be free to co-purify with your protein
or peptide.
HTH,
Javier

On Thu, Sep 20, 2018 at 5:35 PM, Patrick Loll <[email protected]> wrote:

> 1) Use a different protease, e.g. SUMO protease, which is sufficiently
> specific that it’s unlikely to cause any problems even if a little bit is
> carried along. See, for example (shameless plug #1): DOI:
> 10.1016/j.pep.2006.12.006
>
> 2) Use intein cleavage. NEB sells a vector that lets you fuse an intein &
> a CBD at the C-term end of your POI; we’ve made a similar vector with a
> His-tag (shameless plug #2): DOI: 10.1021/ja208755j
>
> 3) Just assure your colleague that you guys are good protein chemists, so
> don’t worry, be happy.
>
> There are chemical cleavage methods (e.g. cyanogen bromide), but they
> aren’t particularly gentle, so if your 110-residue peptide is meant to fold
> into a native structure, I’d approach them with caution (on the other hand,
> if the peptide ISN’T meant to be folded, then just purify via
> reverse-phase, and you’ll for sure get rid of protease contaminants).
>
> Pat
>
>
> > On 20 Sep 2018, at 4:17 PM, Gloria Borgstahl <[email protected]>
> wrote:
> >
> > Hello, friends in crystallography,
> > A colleague just asked me this question.  He is worried about trace
> > protease interfering with the receptors he is studying in cell-based
> > experiments using a 110 amino acid protein we made for him.  He has
> > been unable to make the peptide synthetically.  The company is having
> > trouble getting that to happen.  Any ideas?  Happy Thursday, G
> >
> > ########################################################################
> >
> > To unsubscribe from the CCP4BB list, click the following link:
> > https://www.jiscmail.ac.uk/cgi-bin/webadmin?SUBED1=CCP4BB&A=1
>
> ------------------------------------------------------------
> ---------------------------
> Patrick J. Loll, Ph. D.
> Professor of Biochemistry & Molecular Biology
> Drexel University College of Medicine
> Room 10-102 New College Building
> 245 N. 15th St., Mailstop 497
> Philadelphia, PA  19102-1192  USA
>
> (215) 762-7706
> [email protected]
> [email protected]
>
> ########################################################################
>
> To unsubscribe from the CCP4BB list, click the following link:
> https://www.jiscmail.ac.uk/cgi-bin/webadmin?SUBED1=CCP4BB&A=1
>



-- 
Dr. Javier M. González
Instituto de Bionanotecnología del NOA (INBIONATEC-CONICET)
Universidad Nacional de Santiago del Estero (UNSE)
RN9, Km 1125. Villa El Zanjón. (G4206XCP)
Santiago del Estero. Argentina
Tel: +54-(0385)-4238352
Email <[email protected]> LinkedIn
<https://www.linkedin.com/in/javier-m-gonzalez-inbionatec>

########################################################################

To unsubscribe from the CCP4BB list, click the following link:
https://www.jiscmail.ac.uk/cgi-bin/webadmin?SUBED1=CCP4BB&A=1

Reply via email to