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Expression and Purification of Soluble Non-Fusion Vasostatin in Escherichia coli

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Abstract:

Vasostatin has previously been expressed in fused form or in inclusion body form in Escherichia coli. Here the protein was expressed in soluble non-fusion form in BL21(DE3)pLysS by IPTG induction. The expression level of vasostatin was about 15% of the total cellular protein. The expressed vasostatin was purified and its biological activity was investigated by an endothelial cell proliferation assay.

Keywords: purification; soluble expression; vasostatin

Document Type: Review Article

DOI: http://dx.doi.org/10.2174/0929866054696163

Affiliations: Biopharmaceutical Research & Development Center, Pharmacy College, Jinan University, Guangzhou 510632, P. R. China;

Publication date: October 1, 2005

More about this publication?
  • Protein & Peptide Letters publishes short papers in all important aspects of protein and peptide research, including structural studies, recombinant expression, function, synthesis, enzymology, immunology, molecular modeling, drug design etc. Manuscripts must have a significant element of novelty, timeliness and urgency that merit rapid publication. Reports of crystallisation, and preliminary structure determinations of biologically important proteins are acceptable. Purely theoretical papers are also acceptable provided they provide new insight into the principles of protein/peptide structure and function.
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