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Suc-Leu-Leu-Val-Tyr-AMC

Proteasome substrate
 
BML-P802-0005 5 mg 81.00 USD
 
Replaces Prod. #: ALX-260-070

Fluorogenic substrate for 20S proteasome (Prod. No. BML-PW8720) and other chymotrypsin-like proteases, as well as calpains. Ex.: 380nm Em.: 460nm.

Product Specification

Alternative Name:Suc-LLVY-AMC, Proteasome substrate (fluorogenic), Calpain substrate (fluorogenic)
 
Sequence:N-Succinyl-Leu-Leu-Val-Tyr-AMC (AMC=7-amino-4-methylcoumarin)
 
Formula:C40 H53 N5 O10
 
MW:763.9
 
CAS:94367-21-2
 
Formulation:Lyophilized.
 
Purity:>97% (HPLC)
 
Solubility:Soluble in DMSO (at least 5mM).
 
Long Term Storage:-20°C
 
Handling:Protect from light.
 

Product Literature References

Marchantin M: a novel inhibitor of proteasome induces autophagic cell death in prostate cancer cells: H. Jiang, et al.; Cell Death Dis. 4, e761 (2013), Application(s): Fluorogenic substrate for kinetics assay of 20S proteasome, Abstract; Full Text
Differential apoptosis-related protein expression, mitochondrial properties, proteolytic enzyme activity, and DNA fragmentation between skeletal muscles: E.M. McMillan, et al.; Am. J. Physiol. Regul. Integr. Comp. Physiol. 300, R531 (2011), Abstract; Full Text

General Literature References

Reovirus-induced apoptosis is preceded by increased cellular calpain activity and is blocked by calpain inhibitors.: R.L. Debiasi et al.; J. Virol. 73, 695 (1999), Abstract;
Kinetic and mechanistic studies on the hydrolysis of ubiquitin C-terminal 7-amido-4-methylcoumarin by deubiquitinating enzymes.: L.C. Dang et al.; Biochemistry 37, 1868 (1998), Abstract;
An alpha-mercaptoacrylic acid derivative is a selective nonpeptide cell-permeable calpain inhibitor and is neuroprotective.: K.K. Wang et al.; Proc. Natl. Acad. Sci. USA 93, 6687 (1996), Abstract;
Kinetic characterization of the chymotryptic activity of the 20S proteasome.: R.L. Stein et al.; Biochemistry 35, 3899 (1996), Abstract;
Modulation of hypoxia-induced calpain activity in rat renal proximal tubules.: C.L. Edelstein et al.; Kidney Int. 50, 1150 (1996), Abstract;
Kinetic studies of isopeptidase T: modulation of peptidase activity by ubiquitin.: R.L. Stein et al.; Biochemistry 34, 12616 (1995), Abstract;
Purification and characterization of a Z-Leu-Leu-Leu-MCA degrading protease expected to regulate neurite formation: a novel catalytic activity in proteasome.: S. Tsubuki et al.; Biochem. Biophys. Res. Commun. 196, 1195 (1993), Abstract;
Comparative specificity and kinetic studies on porcine calpain I and calpain II with naturally occurring peptides and synthetic fluorogenic substrates.: T. Sasaki et al.; J. Biol. Chem. 259, 12489 (1984), Abstract;

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