Have you considered not staining at all when you know you have protein on
your gel? Just slice your gel into small pieces, pixels?, keeping a
record of the location and do in-gel digests on all those "pixels"
followed by LC-MS or MALDI. This was a suggestion from David Arnott from
Genentech at a recent Asilomar conference. Ag does not stain all proteins
equally and at very low levels not at all.. Not staining can also reduce
the contamination level.
-Lowell H. Ericsson, Dept. of Biochemistry, U. of Washington, Seattle, WA
On Thu, 21 Oct 1999, lisa bibbs wrote:
> What is the best stain for sub-pmole amounts of protein to be in-gel
> digested followed by Mass spec identification (MALDI followed by
> LC-MS)? I have heard that Silver staining can be very bad and
> produce no MALDI results. We haven't gone to sub-pmole yet so we
> have just been using Coomassie and such.
>
> Thanks for your help.
>
> Lisa
> Lisa Bibbs, Ph.D.
> 10550 N. Torrey Pines Rd.
> SP3
> La Jolla, CA 92039
>
> http://corefac.scripps.edu
>
>