Soluble high-expression, purification and bioassay of IGFBP-3.
- Author:
Chen WU
1
;
Guang-Yin YAO
;
Min-Ji ZOU
;
Guang-Yu CHEN
;
Min WANG
;
Jia-Xi WANG
;
Dong-Gang XU
Author Information
1. Institute of Basic Medical Sciences, Beijing 100850, China.
- Publication Type:Journal Article
- MeSH:
Blotting, Western;
Cell Line, Tumor;
Cell Proliferation;
drug effects;
Chromatography, Affinity;
Dose-Response Relationship, Drug;
Electrophoresis, Polyacrylamide Gel;
Enzyme-Linked Immunosorbent Assay;
Escherichia coli;
genetics;
Gene Expression;
Humans;
Insulin-Like Growth Factor Binding Protein 3;
genetics;
metabolism;
pharmacology;
Insulin-Like Growth Factor I;
metabolism;
Protein Binding;
Recombinant Proteins;
isolation & purification;
metabolism;
pharmacology;
Solubility
- From:
Chinese Journal of Biotechnology
2007;23(3):398-402
- CountryChina
- Language:Chinese
-
Abstract:
cDNA for Insulin-like growth factor binding protein 3 was cloned and constructed a prokaryotic expression vector--pET-DsBA-IGFBP3. The construct was transformed into E. coli BL21 (DE3)plysS. The induced fusion protein (D-IGFBP3) was expressed successfully in soluble form. We obtained D-IGFBP3 the purify of which is over 95% after purification by His affinity chromatography. The product was identified by Western-blot. The cell assay showed that the obtained fusion protein can inhibit the growth of MCF-7 and bind with IGF-I in vitro.
