General description
An internally quenched fluorogenic substrate peptide derived from the calpain-1 cleavage site of α-spectrin. It is not recognized by trypsin or α-chymotrypsin and serves as a sensitive and specific substrate for calpain-1 (Km = 4.6 µM; kcat = 11 s-1). Cleavage occurs at the Tyr-Gly bond and results in enhanced fluorescence. Excitation max: ~490 nm; emission max: ~518 nm.
An internally quenched fluorogenic substrate peptide derived from the calpain-1 cleavage site of α-spectrin. It is not recognized by trypsin or α-chymotrypsin and serves as a sensitive and specific substrate for calpain-1 (Km = 4.6 µM; kcat = 11 s-1). Cleavage occurs between Tyr-Gly residues and results in enhanced fluorescence.
Biochem/physiol Actions
Cell permeable: no
Primary Target
A sensitive and specific substrate for calpain-1
Product does not compete with ATP.
Reversible: no
Packaging
Packaged under inert gas
Warning
Toxicity: Standard Handling (A)
Sequence
H-Lys(FAM)-Glu-Val-Tyr~Gly-Met-Met-Lys(DABCYL)-OH
Physical form
Supplied as a trifluoroacetate salt.
Reconstitution
Following reconstitution, aliquot and freeze (-20°C). Stock solutions are stable for up to 3 months at -20°C.
Other Notes
Mittoo, S., et al. 2003. Anal. Biochem.319, 234.
Legal Information
CALBIOCHEM is a registered trademark of Merck KGaA, Darmstadt, Germany
- UPC:
- 41116113
- Condition:
- New
- Weight:
- 1.00 Ounces
- HazmatClass:
- No
- WeightUOM:
- LB
- MPN:
- 208748-2MG
