About Caspase 8
This gene encodes a member of the cysteine-aspartic acid protease (caspase) family. Sequential activation of caspases plays a central role in the execution-phase of cell apoptosis. Caspases exist as inactive proenzymes composed of a prodomain, a large protease subunit, and a small protease subunit. Activation of caspases requires proteolytic processing at conserved internal aspartic residues to generate a heterodimeric enzyme consisting of the large and small subunits. This protein is involved in the programmed cell death induced by Fas and various apoptotic stimuli. The N-terminal FADD-like death effector domain of this protein suggests that it may interact with Fas-interacting protein FADD. This protein was detected in the insoluble fraction of the affected brain region from Huntington disease patients but not in those from normal controls, which implicated the role in neurodegenerative diseases. Many alternatively spliced transcript variants encoding different isoforms have been described, although not all variants have had their full-length sequences determined. [provided by RefSeq, Jul 2008]

About Janelia Fluor 646
Janelia Fluor® 646 was developed at the Janelia Campus of the Howard Hughes Medical Institute but is commercialized by other vendors. The Janelia Fluor®s family is unique in that the fluorophores are cell-permeable and are available in photoactivatable forms. These fluorophores were developed for super-resolution microscopy (STED, PALM and STORM) and live-cell microscopy in the HaloTag and SNAP-tag versions. Janelia Fluor® 646 has an excitation peak at 646 nm and an emission peak at 664 nm.