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.
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.
Li
Mingcai
M
Allergy and Inflammation Research Institute, Shantou University Medical College, Shantou, PR China. mcli@stu.edu.cn
Feng
Zuohua
Z
Zhang
Guimei
G
Li
Dong
D
D004926:Escherichia coli / Q000235:genetics / Q000378:metabolism*; D005353:Fibronectins / Q000235:genetics / Q000302:isolation & purification* / Q000378:metabolism*; D015870:Gene Expression / Q000235:genetics; D006801:Humans; D010446:Peptide Fragments / Q000378:metabolism; D015202:Protein Engineering / Q000379:methods*; D017434:Protein Structure, Tertiary; D011994:Recombinant Proteins / Q000737:chemistry / Q000235:genetics / Q000302:isolation & purification* / Q000378:metabolism*; D012995:Solubility
C478562:CH50 recombinant polypeptide; D005353:Fibronectins; D010446:Peptide Fragments; D011994:Recombinant Proteins