ADAM-17 Substrate is a peptide sequence engineered to reflect preferred cleavage motifs of ADAM-17 metalloprotease. Hydrophobic and polar residues flank the scissile bond to tune specificity. Researchers use it in kinetic assays to quantify catalytic efficiency and inhibitor potency. Applications include sheddase-mechanism studies, substrate profiling, and drug-discovery screening.
CAT No: Z10-101-231
Synonyms/Alias:ADAM-17 Substrate; HY-P10174; CS-0912082
ADAM-17 Substrate is a specialized peptide compound designed for the study of ADAM-17 (A Disintegrin and Metalloproteinase 17), a key metalloprotease involved in the proteolytic processing of membrane proteins. As a synthetic peptide sequence engineered to serve as a selective substrate for ADAM-17, it enables precise investigation of enzymatic activity, substrate specificity, and regulatory mechanisms within various biological systems. The compound's biochemical properties make it highly valuable for researchers seeking to elucidate the functional roles of ADAM-17 in cellular signaling, inflammation, and proteolytic pathways. Its use is particularly relevant in the context of understanding ectodomain shedding events and the modulation of cell surface protein composition.
Enzyme Activity Assays: ADAM-17 Substrate is extensively utilized in in vitro enzyme activity assays to quantitatively measure the catalytic function of ADAM-17. By providing a defined peptide sequence that is specifically recognized and cleaved by the protease, it allows for accurate determination of enzymatic kinetics, substrate turnover rates, and inhibitor screening. Researchers often employ fluorescence or chromogenic tags on the substrate to facilitate real-time monitoring of cleavage events, thereby supporting the development and validation of ADAM-17 modulators in basic and translational research settings.
Protease Specificity Studies: The substrate's defined sequence permits detailed analysis of substrate recognition and cleavage site preferences by ADAM-17. By systematically modifying amino acid residues within the peptide, scientists can investigate the structural determinants that govern protease-substrate interactions. Such studies are instrumental in mapping the consensus sequences recognized by ADAM-17, advancing the understanding of its substrate repertoire, and distinguishing its activity from closely related metalloproteases within the ADAM family.
Signal Transduction Research: As ADAM-17 is a pivotal regulator of membrane protein shedding, the substrate supports investigations into the downstream effects of proteolytic processing on cell signaling pathways. Utilizing the peptide in cell-free or cell-based systems, researchers can dissect the contribution of ADAM-17-mediated cleavage to the activation or attenuation of signaling cascades, such as those involving growth factors, cytokines, and adhesion molecules. These insights are critical for unraveling the molecular basis of processes like inflammation, cell migration, and tissue remodeling.
High-Throughput Screening: The robust and reproducible cleavage of this peptide by ADAM-17 makes it an ideal tool for high-throughput screening applications. Pharmaceutical and biotechnology laboratories leverage the substrate in automated assay platforms to identify small-molecule inhibitors or activators of ADAM-17. The ability to rapidly assess compound libraries for modulatory effects on protease activity accelerates early-stage drug discovery and supports the identification of novel chemical probes for mechanistic studies.
Biochemical Characterization of Inhibitors: In addition to primary activity assays, the substrate is employed for detailed biochemical characterization of candidate ADAM-17 inhibitors. By monitoring changes in cleavage efficiency in the presence of test compounds, researchers can determine inhibitor potency, selectivity, and mechanism of action. These studies are essential for validating new chemical entities and optimizing lead compounds targeting ADAM-17, thereby contributing to the advancement of research tools and potential therapeutic strategies in the field of protease biology.
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