High-level expression and secretion of recombinant mouse endostatin by Escherichia coli.

@article{Xu2002HighlevelEA,
  title={High-level expression and secretion of recombinant mouse endostatin by Escherichia coli.},
  author={Ren Y. Xu and Peng Du and J Fan and Qian Zhang and Tsai-Ping Li and Ren-bao Gan},
  journal={Protein expression and purification},
  year={2002},
  volume={24 3},
  pages={453-9}
}
The expression of murine endostatin was achieved by placing its gene downstream of an alkaline phosphatase gene (phoA) promoter. To ensure proper folding and secretion of the recombinant protein, the mouse endostatin was fused with alkaline phosphatase signal peptide. SDS/polyacrylamide gel electrophoresis analysis of the culture medium of recombinant Escherichia coli cells revealed that endostatin was efficiently secreted. The signal peptide was efficiently cleaved during secretion as… CONTINUE READING

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