hakorsmo at facstaff.wisc.edu
Thu Feb 26 10:11:14 EST 1998
We are studying a nuclear protein which binds to a promotor element. We have
identified the protein by Western analysis as a previously described homeodomain protein.
Our problem is to explain the fact that though on Western analysis the protein is 38 kDa, when
the protein in a nuclear extract is UV crosslinked to the appropriate BrdU-substituted oligo,
SDS-PAGE suggests a 60 kDa protein.
Any thoughts on an explanation for this? Crosslinking of both our protein and an
unrelated protein to the DNA seems most likely to us.
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