Live-cell　imaging　of　cell-surface-associated　proteolytic　enzymes　is　crucial　to　understand　their　biological　roles　and　functions　in　both　physiological　and　pathological　processes.　However,　the　complexity　of　the　cell　membrane　environment　increases　difficulties　in　specifically　investigating　targeted　proteolytic　activities　within　the　microenvironment.　Towards　this　end,　a　unique,　photoremovable,　furin-responsive　peptide　probe　that　can　undergo　spatiotemporal　control　through　UV-light　illumination　has　been　designed　and　synthesized　to　aid　in　visualizing　the　activity　of　a　cell-surface-associated　protease　enzyme,　furin,　in　live　cells.　Prior　to　light　irradiation,　the　photolabile　moiety,　4,5-dimethoxy-2-nitrobenzyl,　in　the　peptide　sequence　of　the　reporter　will　block　furin-like　enzymatic　hydrolysis,　and　thus,　no　fluorescence　will　be　observed.　Upon　simple　light　illumination,　photolysis　will　occur,　thereby　revealing　the　uncaged　peptide　probe,　which　can　undergo　enzyme　hydrolysis　and　lead　to　an　increase　in　fluorescence　signal;　this　allows　the　real-time　imaging　of　endogenous　cell-surface-associated　furin-like　enzyme　function　in　living　cells　through　precise　spatial　and　temporal　resolution.