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Updated: Sep 26, 2026
Expression of Recombinant Proteins in the Methylotrophic Yeast Pichia pastoris
Published on: February 25, 2010
[Cloning and eukaryotic expression of human lipocalin-type prostaglandin D synthase in Pichia Pastoris]
Yun Gao1, Yu-Feng Huang, Xin-Yi Xia
1Department of Immunology and Microbiology, Nanjing Medical University, Nanjing, Jiangsu 210029, China.
Objectives:
To express human testis Lipocalin-type prostaglandin D synthase in Pichia Pastoris for further research on biological function and clinical applications.
Methods:
Human testis L-PGDS gene coding region was amplified from plasmid pGEX-2T/htL-PGDS by PCR with a deletion of the signal peptide sequence. The DNA fragment was inserted into pPIC9 to construct yeast expression plasmid followed by transformation of the yeast GS115 strain with electroporation. The recombinant his-tag protein was induced to express by methanol.
Results:
The sequence of the amplified DNA fragment was identical to that of human testis L-PGDS previously reported. The recombinant protein was found with a molecular mass of 27,000 on SDS-PAGE, which was identical to that of native L-PGDS.
Conclusions:
Secretory expression of human L-PGDS was obtained in Pichia Pastoris.
