Biopolym. Cell. 2000; 16(3):229-235.
Structure and Function of Biopolymers
Bacterial expression of full-length and truncated forms of cytokine EMAP-2 and cytokine-like domain of mammalian tyrosyl-tRNA synthetase
1Dubrovsky A. L., 2Brown Jn., 1Kornelyuk A. I., 2Murray J. C., 1Matsuka G. Kh.
- Institute of Molecular Biology and Genetics, NAS of Ukraine
150, Akademika Zabolotnoho Str., Kyiv, Ukraine, 03680 - The University of Nottingham
University ParkNottingham, NG7 2RD, UK
Abstract
DNA fragments encoded full-length cytokine EMAP-2 and cytokine-like domain of mammalian TyrRS and truncated from COOH- and NH2-termini forms were cloned in vector for bacterial expression pET32a. For all clones bacterial overexpression were obtained and full-length forms were purified to homogeneity state by affin chromatography and affinity tag was remove by protease cleavage. Induction of tissue factor for full-length forms was tested. Full-length form of cytokine-like domain of mammalian TyrRS did not interact with polyclonal antibody against EMAP-2 in western-blot analysis. It was concluded that this set of recombinant proteins may be usefull for functional study of these cytokine proteins.
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