Hi all!
I try to co-immunoprecipitate two proteins ...
I immunoprecipitate protein A and blot for protein B. I can see this
protein B in my immunoprecipitation (wonderful! :-)) but also in my
negative control with an unspecific antibody ... and also in the control
with lysate and sepharose G beads but without any antibody.
the signals in the controls are not so strong as in the
immunoprecipitation with the specific antibody.
what can I do to lower this background-signal?
should I use another buffer with another detergent ?
now, I use 2% triton x-100 or NP-40.
thanks a lot!
simone
