[Porcine follistatin cDNA cloning and expression in Escherichia coli]

Sheng Wu Gong Cheng Xue Bao. 2006 Jul;22(4):677-81.
[Article in 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.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Animals
  • Base Sequence
  • Cloning, Molecular
  • Escherichia coli / genetics*
  • Follistatin / chemistry
  • Follistatin / genetics*
  • Molecular Sequence Data
  • Phylogeny
  • Recombinant Fusion Proteins / biosynthesis*
  • Swine

Substances

  • Follistatin
  • Recombinant Fusion Proteins