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1. Soluble Expression in Escherichia coli of Active Human Cyclic Nucleotide Phosphodiesterase Isoform 4B2 in Fusion with Maltose-Binding Protein.

Author

Sha Zhu, Genqing Yang, Xiaolan Yang, Yunsheng Zhao, Xiang Li, Ping Deng, Yanling Xie, Zhiyong Gan, Yin Liu, Zhirong Li, Liao, Juan, Ming'an Yu, and Fei Liao

Subjects
*ADENOSINE monophosphate, *EUKARYOTIC cells, *ESCHERICHIA coli, *MALTOSE, *PROTEIN analysis, *PHYSIOLOGY
Abstract

The article focuses on a research about the human cyclic nucleotide phosphodiesterase 4B2's recombinant expression (RE) in Escherichia coli. It cites adenosine 3',5'-cyclic monophosphate (cAMP) as a signal suppressing function of immune cells. It states that human PDE4 can be generated via RE. The significance of the expression in E. coli of eukaryotic genes in fusion with maltose-binding-protein (MBP) and the expression of MBP-hPDEB2 as a soluble active protein in E. coli are also discussed.

Published
2009
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