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Dnp-PLALWAR
| Catalog Number | A18-0038 |
| Category | Fluorescent Enzyme Substrates |
| Molecular Formula | C46H65N13O12 |
| Molecular Weight | 992.1 |
* Please be kindly noted products are not for therapeutic use. We do not sell to patients.
Product Introduction
Dnp-PLALWAR is a fluorogenic substrate for matrix metalloproteinase-1 (MMP-1) and MMP-8. The activity of MMP-1 and MMP-8 can be quantified by measuring tryptophan fluorescence that is unquenched upon peptide hydrolysis that removes the N-terminal dinitrophenol (Dnp) group.
Chemical Information
Product Specification
Application
| Synonyms | Matrix Metalloproteinase-1 Fluorogenic Substrate I; MMP-1 Fluorogenic Substrate I; 1-(2,4-dinitrophenyl)-L-prolyl-L-leucyl-L-alanyl-L-leucyl-L-tryptophyl-L-alanyl-L-arginine |
| Purity | ≥95% |
| Storage | Store at -20°C |
Dnp-PLALWAR is a synthetic fluorogenic peptide substrate specifically designed for the quantitative analysis of matrix metalloproteinases, particularly MMP-1 and MMP-8. The substrate consists of a peptide sequence linked to an N-terminal dinitrophenol (Dnp) group, which acts as a quencher. Upon cleavage by MMP-1 or MMP-8, the removal of the Dnp group results in the unquenching of tryptophan fluorescence, thereby providing a measurable signal to quantify enzyme activity. Dnp-PLALWAR’s design facilitates a straightforward and reliable method for assessing the enzymatic activity of these specific MMPs in various biochemical assays.
One key application of Dnp-PLALWAR is in drug discovery, particularly in screening for inhibitors against MMP-1 and MMP-8, which are implicated in various pathological conditions including cancer, arthritis, and cardiovascular diseases. By providing a direct measurement of enzyme activity through fluorescence, Dnp-PLALWAR enables researchers to rapidly assess the efficacy of potential MMP inhibitors. This application is crucial for developing new therapeutics aimed at modulating MMP activity, which can lead to novel treatments for diseases characterized by excessive extracellular matrix degradation.
Another important application is in biomedical research, where Dnp-PLALWAR is used to study the physiological roles of MMP-1 and MMP-8. Understanding the functionality and regulation of these enzymes in normal and diseased states can provide insights into tissue remodeling, wound healing, and inflammatory responses. The ability to quantitatively measure MMP activity in biological samples allows researchers to explore the contributions of these enzymes to the dynamic remodeling of the extracellular matrix under various physiological and pathological conditions.
Moreover, Dnp-PLALWAR is utilized in the development of diagnostic assays, where its sensitivity and specificity can be leveraged to detect abnormal MMP activity levels in clinical samples. Elevated MMP activity is often associated with a range of diseases, and using Dnp-PLALWAR-based assays, clinicians can potentially diagnose or monitor the progression of these conditions. This application underscores the peptide’s utility not only in basic research and drug development but also in clinical settings where early detection and monitoring of disease progression are critical.
Finally, in the field of tissue engineering and regenerative medicine, Dnp-PLALWAR provides a powerful tool for monitoring MMP activity during scaffold degradation and tissue regeneration processes. The precise quantification of MMP-1 and MMP-8 activity facilitates the optimization of scaffold materials and the tuning of degradation rates to match tissue growth, thereby enhancing the efficacy of tissue engineering approaches. This application highlights the importance of Dnp-PLALWAR in designing strategies to support tissue repair and regeneration through controlled enzymatic activity.
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