Porcine follistatin cDNA cloning and expression in Escherichia coli.
- Author:
Xin HE
1
;
Bing QI
;
Li-Qian HE
;
Yong-Fu CHEN
;
Gui-Sheng LIU
;
Qing-Xuan CHEN
Author Information
1. Institute of Genetics and Developmental Biology, Chinese Academy of Sciences, Beijing 100080, China.
- Publication Type:Journal Article
- MeSH:
Amino Acid Sequence;
Animals;
Base Sequence;
Cloning, Molecular;
Escherichia coli;
genetics;
Follistatin;
chemistry;
genetics;
Molecular Sequence Data;
Phylogeny;
Recombinant Fusion Proteins;
biosynthesis;
Swine
- From:
Chinese Journal of Biotechnology
2006;22(4):677-681
- CountryChina
- Language:Chinese
-
Abstract:
The total RNA was extracted from porcine ovary. Porcine Follistatin cDNA was cloned by RT-PCR. Complete porcine follistatin cDNA coding sequences are presented including 1038 bp of open reading frame. The purified porcine follistatin cDNA was inserted into pGEX-4T-3 vector to construct the prokaryotic fusion protein expression vector. The recombinant expression plasmid was transformed into BL21 (DE3) and expression was induced by IPTG. Protein products were detected by SDS-PAGE and confirmed by Western blotting analysis, which showed that the yield of the Follistatin cDNA was a 63kD protein expression vector. Follistatin protein was expressed in the form of glutathione-S-transferase (GST) fusion protein in E. coli.
