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A new method has been developed for efficient production of soluble proteins in a cell‐free synthesis system. This method involves the use of an engineered ubiquitin sequence as an N‐terminal sequence element that enhances both the productivity and solubility of recombinant proteins. Recombinant proteins were produced with their native amino acid sequences through in situ removal of ubiquitin during cell‐free synthesis reactions in the presence of a deubiquitinase. The presented strategy could be employed as a facile route to prepare soluble proteins required for various applications. This is reported by Devi Kasi, Hee Ju Nah, Christy Catherine, Eung‐Soo Kim, Kyubeom Han, Jong‐Cheon Ha and Dong‐Myung Kim, article number 1700125.
Original Article: Cover Picture: Biotechnology Journal 11/2017NEXT ARTICLE
Recombinant DNA is the formation of a novel DNA sequence by the formation of two DNA strands. These are taken from two different organisms. These recombinant DNA molecules can be made with recombinant DNA technology. The procedure is to cut the DNA of ...