描 述：Highly sensitive and selective cathepsin E FRET substrate derived from the cleavage site sequence of human α2-macroglobulin (Km = 1.9 µM; kcat/Km = 10.2 µM⁻¹s⁻¹ for human erythrocyte cathepsin E). The substrate was resistent to hydrolysis by the analogous aspartic proteinases cathepsin D and pepsin, as well as the lysosomal cysteine proteinases cathepsin B, L, and H. Useful for monitoring and accurately quantifying cathepsin E, even in crude enzyme preparations (excitation wavelength at 328 nm, emission wavelength at 393 nm).
