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Z-LLL-AMC | CAS 152015-61-7
| Catalog Number | A18-0063 |
| Category | Fluorescent Enzyme Substrates |
| Molecular Formula | C36H48N4O7 |
| Molecular Weight | 648.8 |
| Catalog Number | Size | Price | Quantity |
|---|---|---|---|
| A18-0063 | -- | -- |
* Please be kindly noted products are not for therapeutic use. We do not sell to patients.
Product Introduction
Z-LLL-AMC is a fluorogenic substrate for the chymotrypsin-like activity of the 26S proteasome or 20S proteolytic core. AMC (7-amino-4-methylcoumarin) is released to quantify the chymotrypsin-like activity.
Chemical Information
Product Specification
Application
| Synonyms | N-[(phenylmethoxy)carbonyl]-L-leucyl-L-leucyl-N-(4-methyl-2-oxo-2H-1-benzopyran-7-yl)-L-leucinamide; Z-Leu-Leu-Leu-7-amido-4-Methylcoumarin; Proteasome Substrate I |
| Purity | ≥98% |
| Canonical SMILES | CC1=CC(=O)OC2=C1C=CC(=C2)NC(CC(C)C)C(=O)NC(=O)C(CC(C)C)NC(=O)C(CC(C)C)NC(=O)OCC3=CC=CC=C3 |
| InChI | InChI=1S/C36H48N4O7/c1-21(2)15-28(37-26-13-14-27-24(7)18-32(41)47-31(27)19-26)34(43)40-35(44)29(16-22(3)4)38-33(42)30(17-23(5)6)39-36(45)46-20-25-11-9-8-10-12-25/h8-14,18-19,21-23,28-30,37H,15-17,20H2,1-7H3,(H,38,42)(H,39,45)(H,40,43,44)/t28-,29-,30-/m0/s1 |
| InChIKey | MBZJQSNQQJWUBH-DTXPUJKBSA-N |
| Appearance | Solid Powder |
| Excitation | 340-360 nm |
| Emission | 440-460 nm |
| Storage | Store at -20°C |
Z-LLL-AMC, a fluorogenic peptide substrate commonly utilized in biochemical research and diagnostics, showcases a diverse range of applications. Here are four key applications of Z-LLL-AMC:
Protease Activity Assays: At the forefront of protease research, Z-LLL-AMC stands as a pivotal tool for assessing protease activity in diverse biological samples. Upon cleavage by specific proteases, the release of the AMC moiety generates a fluorescent signal, enabling precise quantitative measurements. This method not only facilitates the study of enzyme kinetics but also offers valuable insights into the efficacy of protease inhibitors, shedding light on the intricate functions of these enzymes.
Drug Discovery: Embedded in the realm of pharmaceutical innovation, Z-LLL-AMC emerges as a critical component in the screening of potential protease inhibitors. By monitoring shifts in fluorescence intensity, researchers can pinpoint and characterize compounds that effectively hinder protease activity. This application plays a pivotal role in the development of cutting-edge therapeutic agents aimed at combating protease-associated diseases.
Cancer Research: Within the sphere of cancer investigation, Z-LLL-AMC serves as a cornerstone for exploring the involvement of proteases in tumor progression and metastasis. Through the evaluation of protease activity in cancer cells and tissues, scientists can glean profound insights into tumor biology, uncover potential biomarkers, and identify promising therapeutic targets. This approach aids in unraveling the intricate molecular mechanisms underpinning cancer development and progression.
Apoptosis Studies: In the realm of apoptosis exploration, Z-LLL-AMC emerges as a critical tool for detecting caspase activity, a defining feature of programmed cell death. By monitoring caspase activity through the cleavage of Z-LLL-AMC, researchers can probe apoptotic pathways and assess the impact of pro- and anti-apoptotic agents. This knowledge plays a pivotal role in the development of innovative strategies to modulate cell death in diseases like cancer and neurodegeneration.
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