A very sensitive fluorogenic calpain substrate, Abs/Em=501/527 nm. In general, Rh110-based protease substrates are much more sensitive than the analogous AMC or AFC-based substrate. This enhanced sensitivity might be attributed to the greater fluorescence of the enzymatic product. The colorless and nonfluorescent (Z-Ala-Ala)2Rh110 is hydrolyzed to the highly fluorescent Rhodamine 110, which exhibits excellent spectral properties that match the optimal detection window of most fluorescence instruments. Alternatively, (Z-Ala-Ala)2Rh110 can also be used to detect calpain in a chromogenic mode since the enzymatic product (Rhodamine 110) exhibits a large extinction coefficient (close to 100,000 cm-1mol-1). After cleavage, Abs(max) is at 497 nm and Em(max) is at 527 nm.
-20°C desiccated and protected from light
Gitler D and Spira ME (1998). Real time imaging of calcium-induced localized proteolytic activity after axotomy and its relation to growth cone formation. Neuron 20, 1123-35, Rothe G, et al. (1992). Flow cytometric analysis of protease activities in vital cells. Biol Chem Hoppe Seyler 373, 547-54, Rothe G, et al. (1992). Flow cytometric analysis of protease activities in vital cells. Biol Chem Hoppe Seyler 373, 547-54.