Suc-Leu-Leu-Val-Tyr-AMC (CAS 94367-21-2)
See product citations (3)
QUICK LINKS
Suc-Leu-Leu-Val-Tyr-AMC is a fluorogenic peptide substrate used extensively in biochemistry and molecular biology research for the assay and characterization of protease activity, particularly the proteasome, a protein complex responsible for degrading unneeded or damaged proteins by proteolysis. This substrate is designed to release a fluorescent product upon cleavage by the targeted protease, allowing researchers to monitor protease activity in real time with high sensitivity. The utilization of such substrates facilitates the study of enzyme kinetics and the understanding of protease regulation in various cellular processes, including the ubiquitin-proteasome pathway, which is critical for protein homeostasis within the cell. By providing a quantifiable readout, Suc-Leu-Leu-Val-Tyr-AMC aids in identifying factors that influence protease function and in characterizing the specificity and efficiency of proteasomal enzymes.
Suc-Leu-Leu-Val-Tyr-AMC (CAS 94367-21-2) References
- Characterization of peptidyl boronic acid inhibitors of mammalian 20 S and 26 S proteasomes and their inhibition of proteasomes in cultured cells. | Gardner, RC., et al. 2000. Biochem J. 346 Pt 2: 447-54. PMID: 10677365
- Water modulation of stratum corneum chymotryptic enzyme activity and desquamation. | Watkinson, A., et al. 2001. Arch Dermatol Res. 293: 470-6. PMID: 11758790
- Human platelet 20S proteasome: inhibition of its chymotrypsin-like activity and identification of the proteasome activator PA28. A preliminary report. | Ostrowska, H., et al. 2003. Platelets. 14: 151-7. PMID: 12850839
- Identification, purification, and characterization of a protein activator (PA28) of the 20 S proteasome (macropain). | Ma, CP., et al. 1992. J Biol Chem. 267: 10515-23. PMID: 1587832
- Site-specific degradation of myelin basic protein by the proteasome. | Belogurov, AA., et al. 2009. Dokl Biochem Biophys. 425: 68-72. PMID: 19496324
- Effect of substrate on Ca2(+)-concentration required for activity of the Ca2(+)-dependent proteinases, mu- and m-calpain. | Barrett, MJ., et al. 1991. Life Sci. 48: 1659-69. PMID: 2016996
- Crosstalk between calpain activation and TGF-β1 augments collagen-I synthesis in pulmonary fibrosis. | Li, FZ., et al. 2015. Biochim Biophys Acta. 1852: 1796-804. PMID: 26071646
- Protease Ti from Escherichia coli requires ATP hydrolysis for protein breakdown but not for hydrolysis of small peptides. | Woo, KM., et al. 1989. J Biol Chem. 264: 2088-91. PMID: 2644253
- The first characterization of a eubacterial proteasome: the 20S complex of Rhodococcus. | Tamura, T., et al. 1995. Curr Biol. 5: 766-74. PMID: 7583123
- Evidences for the presence of chymotrypsin-like activity in human spermatozoa with a role in the acrosome reaction. | Morales, P., et al. 1994. Mol Reprod Dev. 38: 222-30. PMID: 8080652
- Mechanistic studies on the inactivation of the proteasome by lactacystin: a central role for clasto-lactacystin beta-lactone. | Dick, LR., et al. 1996. J Biol Chem. 271: 7273-6. PMID: 8631740
- Kinetic characterization of the chymotryptic activity of the 20S proteasome. | Stein, RL., et al. 1996. Biochemistry. 35: 3899-908. PMID: 8672420
- Phosphorylation of the proteasome activator PA28 is required for proteasome activation. | Li, N., et al. 1996. Biochem Biophys Res Commun. 225: 855-60. PMID: 8780702
- Induction of the mitochondrial permeability transition as a mechanism of liver injury during cholestasis: a potential role for mitochondrial proteases. | Gores, GJ., et al. 1998. Biochim Biophys Acta. 1366: 167-75. PMID: 9714791
Ordering Information
| Product Name | Catalog # | UNIT | Price | Qty | FAVORITES | |
Suc-Leu-Leu-Val-Tyr-AMC, 5 mg | sc-471159 | 5 mg | $148.00 | |||
Suc-Leu-Leu-Val-Tyr-AMC, 25 mg | sc-471159A | 25 mg | $490.00 | |||
Suc-Leu-Leu-Val-Tyr-AMC, 100 mg | sc-471159B | 100 mg | $1530.00 |