[Porcine follistatin cDNA cloning and expression in Escherichia coli].
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.
He
Xin
X
Institute of Genetics and Developmental Biology, Chinese Academy of Sciences, Beijing 100080, China.
Qi
Bing
B
He
Li-Qian
LQ
Chen
Yong-Fu
YF
Liu
Gui-Sheng
GS
Chen
Qing-Xuan
QX
D000595:Amino Acid Sequence; D000818:Animals; D001483:Base Sequence; D003001:Cloning, Molecular; D004926:Escherichia coli / Q000235:genetics*; D038681:Follistatin / Q000737:chemistry / Q000235:genetics*; D008969:Molecular Sequence Data; D010802:Phylogeny; D011993:Recombinant Fusion Proteins / Q000096:biosynthesis*; D013552:Swine
D038681:Follistatin; D011993:Recombinant Fusion Proteins