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Highly Active and Removable AffinityTagged Lambda Phosphatase

da Phosphatase efficiently dephosphorylated the autophosphorylated tyrosines of EGFRKD (figure 1). Using 45 or 112 units, Lambda Phosphatase completely dephosphorylated 100 ng and 500 ng of EGFRKD (figure 1; lanes 5, 6, 8 and 9). Using a competitor's lambda phosphatase, we observed complete dephosphorylation only when 50 ng of EGFRKD was assayed (figure 1, lane 1). When more units of the competitor's lambda phosphatase were used under the same assay conditions, incomplete dephosphorylation of 100 ng and 500 ng of EGFRKD (lanes 2 and 3) is observed. As positive controls, 500 ng (lane 4) and 100 ng (lane 7) of autophosphorylated EGFRKD were loaded onto the gel and detected by immunoblotting with an antibody to phosphotyrosine, the PY20 monoclonal antibody.

figure 2

After reaction of EGFRKD with Lambda Phosphatase and treatment with the CaM affinity resin to remove the phosphatase, the tyrosine kinase (TK) activity of the EGFRKD was assayed. The ability to assay enzymatic activity of a protein substrate following dephosphorylation and phosphatase removal is a key feature of CBPtagged Lambda Phosphatase. Because many of the proteins that are phosphorylated in cells are kinases, the effect of phosphorylation on their own kinase activity is of great interest. The kinase activity of EGFRKD, as measured by autophosphorylation, was assayed after dephosphorylation by Lambda Phosphatase. A small loss of the EGFRKD due to nonspecific binding to the resin was observed (figure 2, lane 2). The amount of EGFRKD kinase activity is decreased in the presence of competing lambda pho
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