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Open Access Research article

Expression, purification, and characterization of rhTyrRS

Yongjiang Lang12, Yanling Zhang12, Ling Zhan12, Zhe Feng12, Xiushi Zhou12, Min Yu12* and Wei Mo12*

Author Affiliations

1 The Key Laboratory of Molecular Medicine, Ministry of Education, Fudan University, Shanghai, P.R. China

2 The Department of Biochemistry and Molecular Biology, School of Basic Medical Sciences, Fudan University, Shanghai, P.R. China

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BMC Biotechnology 2014, 14:64  doi:10.1186/1472-6750-14-64

Published: 15 July 2014



Aminoacyl-tRNA synthetases (AARSs) catalyze the first step of protein synthesis. Emerging evidence indicates that AARSs may have additional functions, playing a role in signal transduction pathways regulating thrombopoiesis and inflammation. Recombinant human tyrosyl-tRNA synthetase (rhTyrRS) is engineered with a single amino acid substitution that unmasks its cytokine activity. An industrial production method that provides high yield as well as high purity, quality, and potency of this protein is required for preclinical research.


We expressed codon-optimized rhTyrRS in Escherichia coli under fermentation conditions. Soluble protein was purified by a three-step purification method using cation exchange chromatography, gel filtration chromatography, and anion exchange chromatography. We also established a method to test the biological activity of rhTyrRS by measuring aminoacylation and IL-8 release in rhTyrRS-treated HL-60 cells.


The characterization of purified rhTyrRS indicated that this protein can be used in pharmacodynamic and pharmacokinetic studies.

Recombinant human tyrosyl-tRNA synthetase; Expression of rhTyrRS; Protein purification; Biological activity assay