LRRKtide functions as a defined peptide substrate for exploring kinase specificity and phosphorylation kinetics. Residue placement influences charge distribution and local folding. Researchers examine catalytic efficiency and structural adaptability. Applications include signaling-pathway studies, enzyme profiling, and biochemical mechanism mapping.
CAT No: R2480
CAS No:1071466-49-3
Synonyms/Alias:LRRKtide;HY-P5979;DA-55041;CS-0901237;1071466-49-3;
LRRKtide is a synthetic peptide substrate derived from a segment of the human moesin protein, specifically designed for the study of leucine-rich repeat kinase 2 (LRRK2) enzymatic activity. As a well-characterized peptide sequence, it serves as a model substrate in kinase assays, enabling researchers to probe the biochemical properties and regulatory mechanisms of LRRK2, a protein kinase implicated in multiple cellular signaling pathways and neurodegenerative disease research. Its defined amino acid sequence and phosphorylation site make it a valuable biochemical tool for dissecting kinase-substrate interactions, optimizing assay conditions, and evaluating modulators of LRRK2 function in vitro.
Kinase activity assays: LRRKtide is widely utilized as a substrate in in vitro kinase assays to quantitatively assess the phosphorylation activity of LRRK2 and related kinases. By providing a specific phosphorylation site within its sequence, the peptide enables precise measurement of enzyme kinetics, substrate specificity, and catalytic efficiency. Researchers employ it to characterize mutant or wild-type LRRK2 variants, compare kinase activities, and screen for potential kinase inhibitors or activators in a controlled biochemical context.
Inhibitor screening: The peptide substrate plays a central role in high-throughput screening platforms aimed at identifying small molecule inhibitors or modulators of LRRK2. By monitoring the phosphorylation of LRRKtide in the presence of compound libraries, scientists can efficiently evaluate candidate molecules for their ability to modulate kinase activity. This application is particularly relevant in drug discovery pipelines focused on neurodegeneration and other pathologies where dysregulated kinase signaling is implicated.
Phosphorylation site validation: Researchers use LRRKtide to validate the specificity and efficiency of phosphorylation at defined serine or threonine residues. Its sequence is engineered to contain a consensus motif recognized by LRRK2, allowing for detailed studies of substrate recognition and site preference. Such validation is essential for elucidating the molecular determinants of kinase-substrate interactions and for developing more selective biochemical assays.
Assay development and optimization: The defined properties of LRRKtide make it a preferred standard when developing and optimizing kinase assay protocols. Its reproducible response to phosphorylation facilitates the calibration of detection methods such as radiometric, fluorescence-based, or mass spectrometry assays. Scientists can systematically adjust assay conditions, such as buffer composition and cofactor concentrations, using the peptide as a reliable benchmark for assay performance and reproducibility.
Mechanistic studies of kinase regulation: LRRKtide serves as a practical model for investigating the regulatory mechanisms governing LRRK2 activity, including the effects of post-translational modifications, protein-protein interactions, or allosteric modulators. By providing a consistent and accessible substrate, it enables detailed mechanistic analyses that inform our understanding of kinase regulation, substrate selection, and signal transduction pathways. These studies contribute fundamental insights into the broader roles of kinases in cellular physiology and disease mechanisms.
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