@article{Phuong_Tuteja_Ham_Hoi_2012, title={Expression and purification of recombinant protein NLI-IF from Escherichia coli}, volume={34}, url={https://vjs.ac.vn/index.php/vjbio/article/view/2468}, DOI={10.15625/0866-7160/v34n3.2468}, abstractNote={<p>In order to investigate the expression level of NLI-IF (Nuclear LIM Interactor-Interacting Factor) transcription factor - encoding gene which involved in drought tolerance in rice and identiflied<em> in vitro </em>DNA - binding ability of NLI-IF, we expressed and purified recombinant protein NLI-IF from <em>E. coli</em> Rossetta. ­1,3 kb NLI-IF - encoding sequence was cut from pGEMT/NLI-IF and inserted into <em>Eco</em>RI/<em>Xho</em>I site in MCS of expression vector pET28a. pET28a/NLI-IF was transformed into <em>E. coli</em> Rossetta. 52 kDa recombinant protein NLI-IF was expressed optimally in <em>E. coli </em>using 0.1 mM IPTG as an inducer, at 20<sup>o</sup>C, for 5 h. We were successful in purification of recombinant protein NLI-IF using Ni-NTA affinity chromatography systerm. Purified protein has an ability of binding, specifically, to anti-His-tag antibody in Westerrn blot assay.</p>}, number={3}, journal={Academia Journal of Biology}, author={Phuong, Nguyen Duy and Tuteja, Najaren and Ham, Le Huy and Hoi, Pham Xuan}, year={2012}, month={Oct.}, pages={347–353} }