AMARA peptide (TFA) is a substrate for salt-inducible kinase (SIK) and adenosine monophosphate activated protein kinase (AMPK).
CAT No: R1185
AMARA peptide TFA is a synthetic peptide composed of the amino acid sequence Ala-Met-Ala-Arg-Ala, supplied as its trifluoroacetate salt. As a well-characterized substrate for protein kinases, particularly AMP-activated protein kinase (AMPK), this pentapeptide has earned a central role in signal transduction research and kinase assay development. Its defined sequence and high solubility make it an ideal tool for in vitro biochemical studies, enabling precise investigation of phosphorylation events and substrate specificity. The AMARA peptide is widely recognized for its utility in dissecting the mechanisms of cellular energy regulation and metabolic signaling pathways.
Kinase activity assays: Utilization of the AMARA peptide as a substrate in kinase assays is a foundational application in enzymology research. Owing to its optimal recognition by AMPK and related kinases, the peptide allows researchers to quantitatively assess kinase activity by measuring phosphate incorporation. Its defined sequence ensures reproducibility and sensitivity, facilitating the development of robust assay platforms for high-throughput screening, inhibitor profiling, and mechanistic studies of kinase regulation.
Signal transduction studies: The peptide is instrumental in unraveling the intricacies of cellular signaling cascades, particularly those involving the AMPK pathway. By serving as a model substrate, it enables the evaluation of upstream and downstream modulators that influence phosphorylation dynamics. Researchers leverage this property to elucidate the effects of small molecules, protein-protein interactions, and post-translational modifications on kinase-mediated signaling, thereby advancing understanding of metabolic homeostasis and cellular stress responses.
Enzyme kinetics and specificity analysis: The AMARA sequence provides a reliable framework for detailed kinetic studies, allowing precise determination of parameters such as Km and Vmax for various kinases. Its use in specificity profiling helps distinguish between closely related kinase isoforms and assesses the impact of sequence modifications on substrate affinity. This level of analysis is vital for designing selective inhibitors and for characterizing the substrate preferences of novel or engineered kinases.
Peptide-based inhibitor screening: In drug discovery and chemical biology, the peptide serves as a reference substrate in competitive assays to identify and characterize small molecule inhibitors targeting kinase activity. By monitoring changes in phosphorylation efficiency in the presence of candidate compounds, researchers can rapidly evaluate inhibitor potency, selectivity, and mechanism of action. This approach accelerates the identification of lead compounds for further development in metabolic and signaling research.
Analytical method validation: The defined physicochemical properties and predictable phosphorylation profile of the peptide make it an excellent standard for validating analytical techniques such as high-performance liquid chromatography (HPLC), mass spectrometry, and capillary electrophoresis. Its use in method development ensures accurate quantification and detection of phosphorylated species, supporting rigorous quality control and reproducibility in biochemical investigations.
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