Time-resolved fluorescence microscopy is the ultimate tool to study dynamic events in cellular structures and nanomaterials. Unlike conventional intensity based fluorescence microscopy, fluorescence lifetime is an intrinsic property of a fluorophore, and therefore its measurement is not affected by non-uniform loading, photobleaching, excitation light instability, and light scattering. More importantly, time-resolved measurements can provide essential dynamic information about a fluorophore’s microenvironment and its interaction with other molecules. HORIBA Scientific, the leader in fluorescence spectroscopy, offers the DeltaMyc™, a filter-based confocal microscope system to measure fluorescence lifetime and intensity in micro scales.   
   
The DeltaMyc features time-correlated single photon counting (TCSPC) for sensitive and rapid acquisition of luminescence lifetimes from 100 ps to seconds. It is composed of a compact optical module added to an Olympus BX 53 upright microscope or IX73 inverted microscope. Its mapping capabilities include an automated X,Y fast scanning stage, which combined with its confocal ability, can generate fluorescence lifetime mapping with micron level spatial resolution.   
   
The DeltaMyc is a flexible research tool that combines a large range of picosecond pulsed laser diode sources spanning wavelengths from 370 to 980 nm and repetition rates from CW to 100 MHz, multiple filter configurations and various detector options to suit your specific measurement needs. An included high dynamic range, low noise, cooled camera and a high intensity fluorescence illuminator configured with the DeltaMyc enable widefield fluorescence imaging.   
   
The DeltaMyc features fully-automated mapping controlled from the intuitive user interface of our DataStation software, while retaining the full flexibility and functionality of the microscope. Full reconvolution analysis can be performed to generate maps of the fit parameters such as lifetimes, relative amplitudes, average lifetime, and fluorescence intensity. For example, it is ideal an instrument study protein dynamics such as binding or disassociation using Fluorescence Resonance Energy Transfer (FRET).