Two-hybrid screening developed in a silkworm cell line from the larva or caterpillar of the domesticated silk moth, "Bombyx mori" (BmN4 cells). This system uses the GAL4 BD and the activation domain of mouse NF-κB P65. Both are under the control of the OpIE2 promoter. By changing specific amino acids by mutating the corresponding DNA base-pairs in the plasmids used, the importance of those amino acid residues in maintaining the interaction can be determined. After using bacterial cell-based method to select DNA-binding proteins, it is necessary to check the specificity of these domains as there is a limit to the extent to
Serratiopeptidase Serratiopeptidase Serratiopeptidase (Serratia E-15 protease, also known as serralysin, serrapeptase, serratiapeptase, serratia peptidase, serratio peptidase, or serrapeptidase) is a proteolytic enzyme (protease) produced by non-pathogenic enterobacterium "Serratia" sp. E-15. This microorganism was originally isolated in the late 1960s from silkworm "Bombyx mori" L. (intestine), Serratiopeptidase is present in the silkworm intestine and allows the emerging moth to dissolve its cocoon. Serratiopeptase is produced by purification from culture of Serratia E-15 bacteria. Some alternative medicine proponents claim that serratiopeptidase is beneficial for pain and inflammation but "existing trials [have been] small and generally of poor methodological quality." Online medical journal "Bandolier"