当社グループは 3,000 以上の世界的なカンファレンスシリーズ 米国、ヨーロッパ、世界中で毎年イベントが開催されます。 1,000 のより科学的な学会からの支援を受けたアジア および 700 以上の オープン アクセスを発行ジャーナルには 50,000 人以上の著名人が掲載されており、科学者が編集委員として名高い
。オープンアクセスジャーナルはより多くの読者と引用を獲得
700 ジャーナル と 15,000,000 人の読者 各ジャーナルは 25,000 人以上の読者を獲得
Dr. Asaduaman1 *, Lutfun Nahar2 , Md. Bakhtiar Lijon3 , Shehen Imrn4 and Mohammad Saedur Rhamane5
Affinity Tags have been performed as the potential tools in the basic biological research field especially for production of recombinant protein and functional proteomics. Those affinity tags were wildly applied to simplify the purification of recombinant protein as well as differentiation of protein complex. Glutathione-S-Transferase (GST) tag has been extensively used in affinity chromatography for purification of fusion/recombinant protein to analysis of structure and function of protein, protein-protein interaction and to produce pharmaceutical product. In this review we describe the advantage of GST-tag in affinity chromatography technique as a method for inducible, high level protein expression and purification of recombinant protein. Recombinant protein which is expressed in a pGEX or pET vectors and that protein with GST-tag encoded at the NH2 - or COOH- region of genome sequence. There are some expression vectors which has different site to approve for unidirectional insertion of the coding region DNA, promoter, primers, antibiotic, Ori and GST-tag into pGEX vectors. By used reduced glutathione (GSH) during affinity chromatography the GST-tag with recombinant protein is eluted and stored it. Displacement of the GST-tag from the recombinant protein performed by protease enzyme for digestion which is purified by the application of another affinity technique.