Parts

Basic Parts

Part NameDescription
BBa_K5174000: V8 proteaseThis 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 prosequenceCleaves 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 systemFlipGFP 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: EGFPPreferentially 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 ProteaseTEV 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.

Composite Parts

Part NameDescription
BBa_K5174011: TEV Protease activation reporting systemThis part includes a green fluorescent protein for control and a red fluorescent protein that reports TEV protease activity; upon TEV protease activation and cleavage of the target sequence in FlipCherry, the Cherry beta sheets 10-11 self-assemble with Cherry beta sheets 1-9 to emit red fluorescence, which can be observed via ELISA reader, fluorescence microscope, or confocal microscope to determine TEV protease activation status.
BBa_K5174012: V8 Protease activation reporting systemThis part includes a control green fluorescent protein and a red fluorescent protein to report V8 protease activity; when activated, V8 protease cleaves the target sequence in Flipcherry, allowing the β10-11 strand to form a red fluorescent structure with β1-9, detectable via ELISA, fluorescence, or confocal microscopy, indicating protease activation.