Luciferase Yfp Fusion
Luciferase Yfp Fusion - Related Videos
10:03
Multiphoton Microscopy of Cleared Mouse Brain Expressing YFP
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Cited by 11 •
2012
Multiphoton microscopy of whole mouse organs is possible by optically clearing the organ before imaging, but not all protocols preserve the fluorescent signal of fluorescent proteins. Using an optical clearing method with ethanol-based dehydration and benzyl alcohol:benzyl benzoate clearing, we show high-resolution multiphoton images of whole mouse brain expressing YFP.
02:45
Nuclear Fusion
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2020
The process of converting very light nuclei into heavier nuclei is also accompanied by the conversion of mass into large amounts of energy, a process called fusion. The principal source of energy in the sun is a net fusion reaction in which four hydrogen nuclei fuse and ultimately produce one helium nucleus and two positrons. A helium nucleus has a mass that is 0.7% less than that of four hydrogen nuclei; this lost mass is converted into energy during the fusion. This reaction produces about...
12:19
Antibody Profiling by Luciferase Immunoprecipitation Systems (LIPS)
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Cited by 146 •
2009
The technical aspects of performing LIPS (Luciferase Immunoprecipitation Systems) are described. The overall approach involves expressing chimeric genes encoding antigens fused to Renilla luciferase (Ruc) in mammalian cells. Crude Ruc-antigen extracts are then prepared and, without purification, employed in immunoprecipitation assays to quantify antibodies.
02:38
An Assay to Evaluate the Effect of Test Compounds on Viral Entry and Fusion in Host Cells
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2025
This video demonstrates an assay to evaluate antiviral agents that target specific steps of the viral entry into host cells and fusion with the endosome. The cells are incubated at a low temperature and then infected with HCV. The low temperature permits viral binding to host cells but inhibits internalization via endocytosis. The test antiviral compound is added, and the cells are incubated at physiological temperature. This shift to a higher temperature facilitates viral entry and allows...
09:27
Generation of Fluorescent Protein Fusions in Candida Species
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Cited by 6 •
2017
PCR-mediated gene modification can be used to generate fluorescent protein fusions in Candida species, which facilitates visualization and quantitation of yeast cells and proteins. Herein, we present a strategy for constructing a fluorescent protein fusion (Eno1-FP) in Candida parapsilosis.
FAQs
Bioluminescence resonance energy transfer occurs when luciferase oxidizes its substrate and releases energy close enough to YFP for transfer to take place. YFP then contributes yellow fluorescence to the detected output, shifting the signal away from the original luciferase emission. This coupling links an enzymatic reaction to a fluorescence-based readout of activity inside living cells.
Energy transfer depends on luciferase and YFP being nearby within the same fusion protein. Their linked arrangement allows the energy generated by substrate oxidation to reach YFP efficiently, rather than being detected only as luciferase bioluminescence. Consequently, the optical output can report activity associated with the fusion protein and support studies of localization or molecular behavior.
The substrate initiates the light-producing reaction by being oxidized by luciferase. That reaction supplies the bioluminescent energy required for transfer to YFP, so substrate-dependent signal generation connects the biochemical event to the optical measurement. Because the reporter does not require external illumination, researchers can monitor the resulting signal while limiting background fluorescence from excitation light.
A typical experiment uses cells that genetically produce the fusion reporter, followed by addition or availability of the luciferase substrate and optical monitoring of the emitted signal. Researchers can then follow changes associated with gene expression, protein localization, or molecular interactions over time. The genetically encoded format supports measurements in living cells rather than requiring external fluorescent illumination.
The reporter can connect optical changes with gene expression, protein localization, and molecular interactions. In biology research, those readouts help examine cell signaling, protein dynamics, and other real-time processes in living cells. Its combined enzymatic and fluorescent behavior is especially useful when investigators need a measurable signal that follows biological activity without relying on external illumination.
Luciferase YFP Fusion reporters generate measurable optical signals during biological activity, allowing researchers to follow processes as they occur in living cells. The absence of external illumination reduces background fluorescence, which can make signal changes easier to associate with the reporter. This supports applications in studying dynamic signaling events, changing protein behavior, and molecular interactions over time.