Internally quenched substrate for calpain-1 (u-calpain) with optimal cleavage motifs flanking the scissile bond. The enzyme showed a more than 18-fold higher turnover rate for the hydrolysis of this FRET substrate based on the amino acid sequence PLFAER than for EVYGMM a sequence derived from the cleavage site of the natural substrate a-spectrin.
Technical inquiry about: 01-4050532 H-Glu(EDANS)-Pro-Leu-Phe-Ala-Glu-Arg-Lys(DABCYL)-OH
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