Replaces Prod. #: ALX-850-230
A QuantiZyme
TM Assay System - DO NOT FREEZE. Fluorogenic, non-radioactive assay designed to measure chymotrypsin-like protease activity of purified 20S proteasome. This 96-well assay is useful for screening inhibitors and modulators of the 20S proteasome. The kit includes purified, human erythrocyte 20S proteasome (20µg). The Suc-LLVY-AMC fluorogenic peptide substrate supplied with this kit is a proteasome substrate commonly used for measuring chymotrypsin-like peptidase activity. The detection of proteolytic activity is based on the release of free AMC fluorophore and offers the following advantages: non-radioactive, convenient real-time kinetics of substrate cleavage, and excellent sensitivity.
A proteasome inhibitor, epoxomicin, is included as a test inhibitor for screening purposes.
Product Specification
| Quantity: | 96 assays |
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| Kit/Set Contains: | Proteasome 20S (human) (purified) (Prod. No. BML-PW8720)
Suc-Leu-Leu-Val-Tyr-AMC (Prod. No. BML-P802)
Proteasome Assay Buffer (Prod. No. BML-KI340)
Sodium Dodecyl Sulfate (Prod. No. BML-KI341)
Epoxomicin (Prod. No. BML-PI127)
AMC (7-Amino-4-methylcoumarin) Calibration Standard (Prod. No. BML-KI144)
1/2 Volume White Microplates (Prod. No. BML-KI571) |
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| Long Term Storage: | +4°C |
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| Handling: | Do not freeze. |
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General Literature References
Epoxomicin, a potent and selective proteasome inhibitor, exhibits in vivo antiinflammatory activity.: L. Meng et al.; PNAS
96, 10403 (1999),
Abstract;
Full Text
The proteasome, a novel protease regulated by multiple mechanisms.: G. N. DeMartino & C. A. Slaughter; J. Biol. Chem.
274, 22123 (1999),
Abstract;
Full Text
Kinetic studies of the branched chain amino acid preferring peptidase activity of the 20S proteasome: development of a continuous assay and inhibition by tripeptide aldehydes and clasto-lactacystin beta-lactone: T. A. McCormack et al.; Biochemistry
37, 7792 (1998),
Abstract;
Catalytic properties of 26 S and 20 S proteasomes and radiolabeling of MB1, LMP7, and C7 subunits associated with trypsin-like and chymotrypsin-like activities.: J. Reidlinger et al.; J. Biol. Chem.
272, 24899 (1997),
Abstract;
Full Text
Kinetic characterization of the chymotryptic activity of the 20S proteasome.: R. L. Stein et al.; Biochemistry
35, 3899 (1996),
Abstract;
Multicatalytic endopeptidase complex: proteasome.: A. J. Rivett et al.; Methods Enzymol.
244, 331 (1994),
Abstract;