Source:
Generated By: https://synbiohub.org/public/igem/igem2sbol/1
Created by: Raik Gruenberg
Date created: 2010-01-26 12:00:00
Date modified: 2015-08-31 04:08:36
Gaussia princeps Luciferase fragment 1
| Types | DnaRegion |
| Roles | polypeptide_domain Protein_Domain |
| Sequences | BBa_J18928_sequence (Version 1) |
Description
N-terminal fragment of H. gaussia luciferase for PCA.Disulfide bonds:
- likely, many Cys in sequence
Purification
Inouye & Sahara (2008) discuss the purification and in-vitro activity of different Luciferases, including Gaussia. They indicate that Gaussia Luciferase was previously purified from insoluable fractions -- perhaps due to the high Cys content.
Goerke et al (2008) Provide optimized in-vitro expression conditions for Gaussia Luciferase based on tuning the strain from which the cell-free lysate is produced.
References
http://www.ncbi.nlm.nih.gov/pubmed/17099704 Remy I, Michnick SW. (2006) A highly sensitive protein-protein interaction assay based on Gaussia luciferase.
http://nar.oxfordjournals.org/cgi/content/full/27/13/e4#hd1 Maroun M, Aronheim A. (2007) A novel in vivo assay for the analysis of protein-protein interaction. PMID: 10373602
http://www.ncbi.nlm.nih.gov/pubmed/19373229 Tannous BA. (2009) Gaussia luciferase reporter assay for monitoring biological processes in culture and in vivo.
http://www.ncbi.nlm.nih.gov/pubmed/18789309 Inouye S, Sahara Y. (2008) Soluble protein expression in E. coli cells using IgG-binding domain of protein A as a solubilizing partner in the cold induced system.
http://www.ncbi.nlm.nih.gov/pubmed/18555198 Goerke AR, Loening AM, Gambhir SS, Swartz JR. (2008) Cell-free metabolic engineering promotes high-level production of bioactive Gaussia princeps luciferase.
Notes
- gene synthesis
- codon optimized for E. coli