Protein-protein gel shifts

Larry lca1 at cornell.edu
Mon Aug 16 19:32:09 EST 1999


I've been trying (unsuccessfully) to perform a protein-protein
gel shift to estimate the binding activity of my preps.  In 
short, I've been incubating equimolar amounts at room temp 
for 30 minutes, and then loading onto a native 4-12% Tris-Glycine
gel.  However, when I silver-stain, I notice immediately that
the larger protein complex formed forms a tight band, but also
"smears" above which makes it difficult to quantitate how much
bound.  Is there anyway to minimize this band-spreading when
running native gels?  Thanks.





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