H-Glu(EDANS)-Pro-Leu-Phe-Ala-Glu-Arg-Lys(DABCYL)-OH |
| Catalog No.GA22349 |
Internally quenched substrate for calpain-1 (µ-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 α-spectrin.
Products are for research use only. Not for human use. We do not sell to patients.
Cas No.: 1914987-47-5
Sample solution is provided at 25 µL, 10mM.
;)
,-1-7$$$37316672.jpg');)
;)
;)
$$$36806353.jpg');)
;33(7)%EF%BC%9A546-561$$$37156877.jpg');)
;)
;)
;)
%201124-1138.$$$35908550.jpg');)
%20766-780.$$$37100057.jpg');)
%20418-432.$$$36893736.jpg');)
%EF%BC%9A-240-255.$$$35108512.jpg');)
533-545$$$36543525.jpg');)
%201-13.$$$36600053.jpg');)
;)
Internally quenched substrate for calpain-1 (µ-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 P
Average Rating: 5 (Based on Reviews and 33 reference(s) in Google Scholar.)
GLPBIO products are for RESEARCH USE ONLY. Please make sure your review or question is research based.
Required fields are marked with *