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Expression and Purification of Recombinant Proteins That Have Native Amino,,,Acid Sequence

cle also presents purification of the mature cleavage product away from free CBP affinity tag, EK and small amounts of uncleaved fusion protein using Stratagene's Calmodulin Affinity Resin and STI Agarose.)

c-Jun N-Terminal Kinase Activity of CBP-JNK

figure 4

Recombinant CBP-JNK, eluted from the calmodulin affinity resin, was used directly in a protein kinase assay to show that it retained protein kinase activity and substrate specificity. In addition, this fusion protein was able to autophosphorylate and phosphorylate its natural substrate, c-Jun N-terminal kinase (figure 4).

Conclusions

The pCALnEK vector and LIC systems are important new tools for producing proteins with native amino acid sequence. Any desired protein coding sequence can be quickly, efficiently and accurately inserted into the pCALnEK vector by LIC, which permits seamless insertion. Protein expression can be controlled by IPTG, and induced protein can be purified to homogeneity using the CBP purification tag and calmodulin affinity resin. If required, the CBP purification tag can be removed using Stratagene's Enterokinase, yielding a protein with native amino acid sequence. Finally, CBP affinity tag and EK can be removed from the purified protein product using Stratagene's Calmodulin Affinity Resin and Soybean Trypsin Inhibitor Agarose (STI Agarose).

Acknowledgments

The authors would like to thank Quinn Lu, Holly Hogrefe and ChaoFeng Zheng for helpful discussions and Diane Beery for her expertise in preparing graphic art.

REFERENCES

  1. Simcox, T.G., Zheng, C.F., Simcox, M.E., and Vaillancourt, P. (1995) Strategies 8: 4043.

  2. StofkoHahn, R.E., Carr, D.W., and Scott
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