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. 1997 Jul 14;138(1):119–130. doi: 10.1083/jcb.138.1.119

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The kinase activity of Gin4 is activated by phosphorylation. (A) The Gin4 protein was immunoprecipitated from mitotic cells and then split into two samples. One sample was treated with lambda phosphatase (New England Biolabs Inc.), while the other sample was treated identically, but with no added phosphatase. The precipitated protein was then resolved on a 9% SDS-polyacrylamide gel and detected by Western blotting. (B) The Gin4 protein was immunoprecipitated and treated with lambda phosphatase as in A. The immunoprecipitate was then washed with kinase buffer several times and assayed for kinase activity.