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Application> Microscopy - Forster (Fluorescence) Resonance Energy Transfer (FRET) Microscopy
Forster (Fluorescence) Resonance Energy Transfer (FRET) Microscopy
Forster (Fluorescence) Resonance Energy Transfer (FRET) Microscopy Typical fluorescence microscopy techniques rely upon the absorption by a fluorophore of light at one wavelength (excitation), followed by the subsequent emission of secondary fluorescence at a longer wavelength. The excitation and emission wavelengths are often separated from each other by tens to hundreds of nanometers. Using this technique, molecules that are closer together than the optical resolution limit appear to be coincident.
Limitations in determination of the spatial proximity of protein molecules can be overcome by applying Forster (or Fluorescence) Resonance Energy Transfer (FRET) microscopy techniques. FRET occurs between two appropriately positioned fluorophores only when the distance separating them is 8 to 10 nanometers or less. Thus, FRET is well-suited to the investigation of protein interactions that occur between two molecules positioned within several nanometers of each other.
Forster (Fluorescence) Resonance Energy Transfer (FRET) Microscopy Lasers
635 nm Collimated Diode Laser System 5 - 500 mW Output Power