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Updated: Jul 9, 2026
Expression of Recombinant Proteins in the Methylotrophic Yeast Pichia pastoris
Published on: February 25, 2010
[Expression and analysis of recombinant pIL-18 in Pichia pastoris]
Shi-Bin Song1, Zhi-Zhong Jing, Guo-Hu Chen
1Key Laboratory of Veterinary Porasitology of Gansu Province/State Key Laboratory of Veterinary Etiological Biology/Lanzhou Veterinary Research Institute, Chinese Acadarny of Agricultural Science, Lanzhou 730046, China.
Abstract:
The porcine IL-18 gene was amplified from recombinant plasmid pGEM-IL-18 by PCR, then the pPIC9K-IL-18 of fusion expression vector was constructed by inserting IL-18 fragment,and was transformed to GS115 by electroporation, multi-copy recombinant strains were screened by G418. The expression of recombinant fusion protein was induced by methanol, SDS-PAGE was used to analyze expression product, fusion protein was purified by Sephadex G-100 column, bioactivity of IL-18 was measured by MTT assays. Experiment results show fusion protein of pIL-18 secreted by GS115,expression reaches the secretion peak of 160 mg/L at 72 h. We have expressed and purified successfully the recombinant pIL-18 with obvious biological activity in Pichia pastoris.
