A specific proteolytic profile associated with cell death has been recently identified and can be measured in a manner similar to LDH assays [26] . This method employs sequence-specific (Ala-Ala-Phe), fluorogenic or luminogenic peptide substrates delivered directly into assay wells via a buffered vehicle. The proteolytic activities present in viable cells are not detected by this method because normally compartmentalized proteases are not in contact with the impermeant substrates. However, protease(s) released into the culture medium as a result of cell death cleave the substrates releasing a detectible reporting molecule. The fluorescent format of the assay utilizes the highly-efficient rhodamine 110 (R110) fluorophore which is measured in as short as 30 minutes by a fluorometer with 485nm excitation and 520-30nm emission filters [52, 53] . The luminescent format employs an engineered luciferase formulation to detect the luciferin product of cleavage thereby generating a glow-type signal which peaks at 15-20 minutes, stably persists for 3-4 hr, and is measured by standard luminometry.