High-level expression of a recombinant fragment of human fibronectin containing the Cell I-Hep II-IIICS71 domain in Escherichia coli as a soluble protein.

Abstract

Fibronectin (FN) is a major matrix protein that is involved in multiple processes. Its Cell I-Hep II domain is potentially useful in tumor therapy. Here, a recombinant fragment of FN with the Cell I-Hep II-IIICS71 domain, CH/71, was expressed in Escherichia coli. The CH/71 fusion protein consists of Cell I-Hep II domain and 19th to 89th amino acids of IIICS domain of FN. The expression level of CH/71 in E. coli was very high after induction with IPTG. Furthermore, CH/71 protein was largely found in the soluble fraction. It was readily purified by one-step heparin-agarose affinity chromatograph. The ability of CH/71 binding cells was about 8-fold of that of Cell I-Hep II domain FN.

• Authors: Mingcai Li, Zuohua Feng, Guimei Zhang, Dong Li
• Journal: Biotechnology letters (Biotechnol Lett) Vol. 28 Issue 14 Pg. 1141-6 (Jul 2006) ISSN: 0141-5492 [Print] Netherlands
• PMID: 16794767 (Publication Type: Journal Article, Research Support, Non-U.S. Gov't)

Chemical References

• CH50 recombinant polypeptide
• Fibronectins
• Peptide Fragments
• Recombinant Proteins

Topics

• Escherichia coli (genetics, metabolism)
• Fibronectins (genetics, isolation & purification, metabolism)
• Gene Expression (genetics)
• Humans
• Peptide Fragments (metabolism)
• Protein Engineering (methods)
• Protein Structure, Tertiary
• Recombinant Proteins (chemistry, genetics, isolation & purification, metabolism)
• Solubility