Hi,

currently I'm trying to do an EMSA in order to study the presence in a nuclear protein extract of proteins that could interact with a FAM-labelled sequence of interest. The last experiment, which results I attach here, shows the absence of any peculiar shift of sample made by oligo and proteins from 0 to 2,5ug of nuclear extract. Meanwhile I note a band shift only when my oligo is incubated with 5ug of nuclear extract, I see precipitation in the well as well.

I have tried the same experiment using TBE and phosphate buffer as running buffer and gel composition but nothing changed.

Any suggestion?

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