Soluble high-expression, purification and bioassay of IGFBP-3 / 生物工程学报
Chinese Journal of Biotechnology
; (12): 398-402, 2007.
Article
in Zh
| WPRIM
| ID: wpr-328016
Responsible library:
WPRO
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.
Full text:
1
Index:
WPRIM
Main subject:
Pharmacology
/
Protein Binding
/
Solubility
/
Recombinant Proteins
/
Insulin-Like Growth Factor I
/
Enzyme-Linked Immunosorbent Assay
/
Gene Expression
/
Blotting, Western
/
Chromatography, Affinity
/
Insulin-Like Growth Factor Binding Protein 3
Type of study:
Prognostic_studies
Limits:
Humans
Language:
Zh
Journal:
Chinese Journal of Biotechnology
Year:
2007
Type:
Article