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Efficient Cleavage of Fusion Proteins to Yield Native Amino Termini

peptide substrate (see legend to Figure 3 ). As the results in panel B show, the recombinant EK was quantitatively removed when the STI Agarose was added to the absorption step.

Conclusions

Stratagene's pure, high-specific-activity, recombinant EK allows efficient, specific cleavage of fusion proteins over a wide range of conditions. Recombinant EK can be used in conjunction with the Affinity and ESP protein expression and purification systems and, in particular, with the new E. coli fusion vector, pCALnEK, to produce unmodified cloned proteins in high yield. With the introduction of STI Agarose, cleaved recombinant proteins with native amino acid sequence can be efficiently recovered from recombinant EK digests without buffer changes or long incubation times.

REFERENCES
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  3. Zheng, C.F., and Simcox, T.G. (1996) Strategies 9: 2021.

  4. Wyborski, D.L., Bauer, J,C., McGowan, B., Sorge, J.A. and Vaillancourt, P. (1997) Strategies 10: 1517.

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