BBa_K5174000: V8 protease | This enzyme cleaves peptide bonds on the carboxyl side of aspartate and glutamate, aiding bacterial colonization and infection by degrading key proteins, maturing proteases, stabilizing lipases, and inactivating immunoglobulins. |
BBa_K5174001: V8 protease with gluse prosequence | Cleaves peptide bonds after aspartate and glutamate, aiding bacterial colonization and infection by degrading host proteins, maturing other proteases, inactivating inhibitors, cleaving immunoglobulins, and possibly stabilizing secreted lipases. |
BBa_K5174002: FlipGFP β10-11(TEV protease cleavage site) | The FlipGFP β10-11 (TEV cleavage site) is used to test TEV protease cleavage, consisting of six parts and forming a complete fluorescent protein upon cleavage, with fluorescence measured at 488nm excitation and 535nm emission in a MicroplateReader. |
BBa_K5174003: FlipGFP β10-11(V8 protease cleavage site) | The FlipGFP β10-11 (V8 cleavage site) is used to test V8 protease cleavage, consisting of six parts and forming a complete fluorescent protein upon cleavage, with fluorescence measured at 488nm excitation and 535nm emission in a MicroplateReader. |
BBa_K5174004: FlipGFP β10-11(V8 protease short cleavage site) | The FlipGFP β10-11 (V8 short cleavage site) is used to test V8-short protease cleavage, consisting of six parts and forming a complete fluorescent protein upon cleavage, with fluorescence measured at 488nm excitation and 535nm emission in a MicroplateReader. |
BBa_K5174005: FlipGFP β1-9, part of Flip system | FlipGFP β1-9, a key component of the Flip system, assembles with cleaved FlipGFP β10-11 to form a complete fluorescent protein, with in vitro experiments conducted on pET28a with a His tag, and fluorescence measured at 488nm excitation and 535nm emission. |
BBa_K5174007: Flipcherry β1-9-Flipcherry and β10-11(TEV cleavage site) | Preferentially cleaves peptide bonds on the carboxyl-terminal side of aspartate and glutamate, aiding in bacterial colonization and infection by degrading host proteins, maturing proteases, inactivating inhibitors, cleaving immunoglobulins, and stabilizing secreted lipases. |
BBa_K5174008: EGFP | Preferentially cleaves peptide bonds on the carboxyl side of aspartate and glutamate, aiding in bacterial colonization, infection, maturation of proteases, degradation of host proteins, and inactivation of inhibitors. |
BBa_K5174009: Flipcherry β1-9-Flipcherry and β10-11(V8 protease short cleavage site) | Flipcherry β10-11 (V8 protease short cleavage site), a key part of the Flip system, tests V8 protease cleavage; upon cleavage, the flipped beta strand reorients, assembling with Flipcherry β1-9 to form a fluorescent protein, both expressed from pRSFDueT under LacI and T7 promoter control. |
BBa_K5174010: TEV Protease | TEV Protease, a cysteine protease from Tobacco Etch Virus expressed in E. coli, specifically cleaves between Gln and Gly/Ser residues, enabling the Flip system to assemble FlipGFP/Cherry β1-9 and β10-11 into a fluorescent protein in vitro and in vivo. |