About Tripeptidyl-Peptidase I
This gene encodes a member of the sedolisin family of serine proteases. The protease functions in the lysosome to cleave N-terminal tripeptides from substrates, and has weaker endopeptidase activity. It is synthesized as a catalytically-inactive enzyme which is activated and auto-proteolyzed upon acidification. Mutations in this gene result in late-infantile neuronal ceroid lipofuscinosis, which is associated with the failure to degrade specific neuropeptides and a subunit of ATP synthase in the lysosome. [provided by RefSeq, Jul 2008]

About DyLight 488
DyLight™ 488 has an excitation peak at 493 nm and an emission peak at 518 nm and is spectrally similar to Alexa Fluor™ 488, fluorescein and FITC. DyLight™ 488 is most commonly used in flow cytometery, and fluorescence microscopy applications.