Purification of Human Recombinant GATA-1 from Bacteria: Implication for Protein-Protein Interaction Studies |
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Authors: | Zinaida Doubeikovskaia Anne Aries Pierre Jeannesson Francois Morle Alexandre Doubeikovski |
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Affiliation: | Institute Biochemistry and Physiology of Microorganisms, Russian Academy of Sciences, Prospekt Nauki, 5, Pushchino Moscow Region, 142290, Russia. douba@rambler.ru |
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Abstract: | GATA-1 is a key regulator of terminal erythroid differentiation in mammals and birds. The structural and biochemical studies of human GATA-1 (hGATA-1) are limited by the difficulty of its purification in a sufficient amount. Here we describe the procedure for obtaining pure bacterial recombinant hGATA-1 in an active functional state. We demonstrate that this protein may be successfully used for preparing an affinity column, producing GATA-1-specific rabbit polyclonal antibodies, and studying DNA-protein and protein-protein interactions. |
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