Renilla reniformis

Green Fluorescent Protein
Biotinylated Avitag™ fusion (C’terminus)

Renilla reniformis or “sea pansy” is strikingly bioluminescent when disturbed in nature, due to Green Fluorescent Protein. This molecule has become extremely important for modern biological science. The green fluorescent protein obtained from this organism exhibits nearly symmetrical excitation and emission  peaks.

Green Fluorescent Protein of Renilla reniformis was genetically engineered to be produced in E.coli and to contain the Avitag peptide sequence (MW 29,525 daltons).  Avitag peptide (GLNDIFEAQKIEWHE) can be efficiently biotinylated by the E.coli enzyme, biotin ligase.  The peptide can be recognized by AbC agarose.

The Green Fluorescent Protein of Renilla reniformis has a diverse range of uses in from cell biology, drug discovery, biomedical research; high throughput screening (HTS) and fluorescence activated cell sorting (FACS).  Fluorescent proteins expressed in living cells (e.g. fungi, bacteria, animals and plants) can be used to study molecular processes in real time such as dynamics of nuclear division, protein trafficking, etc.  GFPs can also be used for the dynamic monitoring of protein interactions using FRET or BRET technologies.

Specification sheet

References

Labas, Y. A., Gurskaya, N. G., Yanushevich, Y. G., Fradkov, A. F., Lukyanov, K. A., Lukyanov, S. A., and Matz, M. V. 2002. Diversity and evolution of the green fluorescent protein family. Proc. Natl. Acad. Sci. USA. 99:4256-4261.   Bryan, B. J., Szent-Gyorgyi, C. 2001. Luciferases, fluorescent proteins, nucleic acids encoding the luciferases and fluorescent proteins and the use thereof in diagnostics, high throughput screening and novelty items. U.S. Patent No. 6,232,107.   Peelle B, Gururaja TL, Payan DG, Anderson DC. 2001. Characterization and use of green fluorescent proteins from Renilla muelleri and Ptilosarcus guernyi for the humancell display of functional peptides. J Protein Chem. 20: 507-19