Gaussia princeps luciferase is a bioluminescent protein. It is ATP-independent, requiring only coelenterazine and O2 as substrates. This purified protein is fused with Avitag™ peptide which is fully biotinylated (MW 21,616 daltons). Gaussia princeps luciferase provides all the research possibilities of the biotin interaction with Streptavidin AND the applications of bioluminescence.
Gaussia luciferase from Gaussia princeps (a marine copepod) was genetically engineered to be produced in E.coli and to contain the Avitag peptide sequence. Avitag peptide (GLNDIFEAQKIEWHE) can be efficiently biotinylated by the E.coli enzyme, biotin ligase . The peptide can be recognized by Abc antibody.
Besides containing a biotinylated Avitag peptide, Gaussia luciferase has very unique properties as a bioluminescent protein.
Specification Sheet
References:
Serganova I, Moroz E, Moroz M, Pillarsetty N and Blasberg R. (2006) Non-invasive molecular
imaging and reporter genes. Central European Journal of Biology. 1: pp. 88-123.
Tannous BA, Kim DE, Fernandez JL, Weissleder R and Breakefield XO. (2005) Codon-optimized
Gaussia luciferase cDNA for mammalian gene expression in culture and in vivo. Mol. Ther. 11: pp.
435–443.
Verhaegen M and Christopoulos TK. (2002) Recombinant Gaussia luciferase. Overexpression,
purification and analytical application of a bioluminescent reporter for DNA hybridization. Anal. Chem.
74: pp. 4378–4385.