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.
  1. Institute of Molecular Biology and Genetics, NAS of Ukraine
    150, Akademika Zabolotnoho Str., Kyiv, Ukraine, 03680
  2. 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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