Suc-Leu-Leu-Val-Tyr-AMC

Proteasome substrate



BML-P802-0005	5 mg	77.00 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)

Formula:	C₄₀ H₅₃ N₅ O₁₀

MW:	763.9

Purity:	>99% (TLC)

Sequence:	N-Succinyl-Leu-Leu-Val-Tyr-AMC (AMC=7-amino-4-methylcoumarin)

Formulation:	Lyophilized.

CAS:	94367-21-2

Peptide Content:	98%

Solubility:	Soluble in DMSO (at least 5mM).

Long Term Storage:	-20°C

Handling:	Protect from light.

Background / Technical Information:	Please click here for the comprehensive product datasheet.

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;