1. Silver staining.
Yes. The way I would do it (only out of complete desperation) is as
follows: Remove silver from a gel by using Farmer's reducer followed by an
extensive washes with water, soak a gel in electrophoresis buffer
containing 0.2% of SDS (time of soaking would depend on gel thickness: the
thicker a gel the longer the time), and electrotransfer as any other gel.
Be aware that electrotransfer yield may be significantly lower than for a
"normal" gel and due to all the chemical operations related to
staining/destaining many proteins may be partially/completely blocked. If
there is enaugh material to run another gel to do electroblotting, this is
definitely much better choice!
2. Western
No. First, some kind of blocking agent has to be used and usually it
is a protein (or protein mixture). Also, both the primary and secondary
antibody used for Western is, most likely, an IgG and their light chains
will sequence beautifully. I am not aware of any protocols describing
complete stripping af a blot from the blocking agent and antibodies. If
one existed it would strip (extract) the protein of interest, too.
Jacek Mozdzanowski
Bioanalytical Sciences
SmithKline Beecham