TY - JOUR AU - Matsunaga, Satoko AU - Matsuoka, Kazuhiro AU - Shimizu, Kouhei AU - Endo, Yaeta AU - Sawasaki, Tatsuya PY - 2010 DA - 2010/06/04 TI - Biotinylated-sortase self-cleavage purification (BISOP) method for cell-free produced proteins JO - BMC Biotechnology SP - 42 VL - 10 IS - 1 AB - Technology used for the purification of recombinant proteins is a key issue for the biochemical and structural analyses of proteins. In general, affinity tags, such as glutathione-S-transferase or six-histidines, are used to purify recombinant proteins. Since such affinity tags often interfere negatively with the structural and functional analyses of proteins, they are usually removed by treatment with proteases. Previously, Dr. H. Mao reported self-cleavage purification of a target protein by fusing the sortase protein to its N-terminal end, and subsequently obtained tag-free recombinant protein following expression in Escherichia coli. This method, however, is yet to be applied to the cell-free based protein production. SN - 1472-6750 UR - https://doi.org/10.1186/1472-6750-10-42 DO - 10.1186/1472-6750-10-42 ID - Matsunaga2010 ER -