Title: Green Fluorescent Protein
Additional Names: GFP
Literature References: Class of autofluorescent proteins found in bioluminescent coelenterates where they function as energy transfer acceptors, emitting a green fluorescent light (lmax = 509 nm). Acidic globular proteins consisting of 238 amino acids, monomeric mol wt ~30,000. Developed commercially as a biochemical tool to visualize cellular structure and monitor dynamic cellular events via fluorescence resonance energy transfer (FRET) assays. Purifn, characterization and energry transfer studies from Aequorea victoria: H. Morise et al., Biochemistry 13, 2656 (1974); from Renilla reniformis: W. W. Ward, M. J. Cormier, J. Biol. Chem. 254, 781 (1979). Properties of naturally occurring proteins: M. Chalfie, Photochem. Photobiol. 62, 651 (1995). Structural studies of chromophore fragment: G. N. Phillips, Jr., Curr. Opin. Struct. Biol. 7, 821 (1997); B. R. Branchini et al., J. Am. Chem. Soc. 120, 1 (1998). Fluorescence and spectral properties of variants genetically engineered for enhanced fluorescence: G. H. Patterson et al., Biophys. J. 73, 2782 (1997); R. H. Stauber et al., BioTechniques 24, 462 (1998); for Ca2+ visualization: T. Nagai et al., Proc. Natl. Acad. Sci. USA 98, 3197 (2001). Review of expression and detection: S. R. Kain, P. Kitts, Methods Mol. Biol. 63, 305-324 (1997). Review of research applications: T. Misteli, D. L. Spector, Nat. Biotechnol. 15, 961-964 (1997); as reporter gene: S. R. Kain et al., BioTechniques 19, 650-655 (1995); as fluorescent protein tag: H.-H. Gerdes, C. Kaether, FEBS Lett. 389, 44-47 (1996). Bibliography: L. J. Kricka, P. E. Stanley, J. Biolumin. Chemilumin. 12, 113-134 (1997).
Use: Research tool in cell biology. |