Enhanced soluble protein expression using two new fusion tags.

  title={Enhanced soluble protein expression using two new fusion tags.},
  author={Deb K. Chatterjee and Dominic Esposito},
  journal={Protein expression and purification},
  volume={46 1},
Production of soluble recombinant proteins is vital for structure-function analysis and therapeutic applications. Unfortunately, when expressed in a heterologous host, such as Escherichia coli, most proteins are expressed as insoluble aggregates. Two new fusion partners have been identified to address these solubility problems. One of the tags was derived from a bacteriophage T7 protein kinase and the other one from a small E. coli chaperone, Skp. We have expressed a panel of insoluble human… CONTINUE READING

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