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Highly Active and Removable AffinityTagged Lambda Phosphatase

sphatase (figure 2, lane 3). The tyrosine kinase activity of EGFRKD was not adversely affected by one or two CaM resin treatments (figure 2, lanes 4 and 5).

Conclusions

The data presented here demonstrate both the efficient dephosphorylation of substrate by Lambda Phosphatase and the removal of Lambda Phosphatase by CaM affinity resin treatment. Assay of target protein activity after dephosphorylation and phosphatase removal is also shown. These experiments illustrate the usefulness of Stratagene's affinitytagged Lambda Phosphatase for investigating the effects of phosphorylation on substrate protein binding and enzymatic activities.

REFERENCES

  1. Pawson, T. (1994) FASEB J. 8: 11121113.

  2. Hunter, T. (1987) Cell 50: 823829.

  3. Guan, K.L., and Dixon, J.E. (1991) J. Biol. Chem. 266: 1702617030.

  4. Zhou, S., et al. (1993) J. Biol. Chem. 268: 1775417761.

  5. StofkoHahn, R.E., Carr, D.W., and Scott, J.D. (1992) FEBS Lett. 302: 274278.


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