MLCK inhibitor peptide 18 is a cell-permeable inhibitor of myosin light chain kinase (MLCK; IC50 = 50 nM), and displays 4000-fold selectivity over cam kinase ii and does not inhibit PKA. It prevents defects in transepithelial barrier resistance induced by bacteria or TNF-α plus IFN-γ. MLCK inhibitor peptide 18 prevents sperm chromatin-induced cortical reorganization in mouse oocytes and decreases phagocytosis of C3bi-opsonized and non-opsonized myelin by primary mouse microglia.
CAT No: R0854
CAS No:224579-74-2
Synonyms/Alias:MLCK inhibitor peptide 18;224579-74-2;Myosin Light Chain Kinase Inhibitor Peptide 18;CHEMBL443574;peptide 18;H-Arg-Lys-Lys-Tyr-Lys-Tyr-Arg-Arg-Lys-NH2;MLCK Inhibitor Peptide-18;GTPL9351;GLXC-15538;ZIA57974;R-K-K-Y-K-Y-R-R-K-NH2;BDBM50074638;AKOS024456829;DA-65540;G13301;
MLCK inhibitor peptide 18 is a synthetic peptide designed to selectively inhibit myosin light chain kinase (MLCK), a serine/threonine-specific protein kinase that plays a central role in the regulation of actomyosin contractility. By mimicking critical substrate or regulatory sequences, this peptide modulates the phosphorylation state of myosin light chains, thereby influencing cellular contraction, motility, and cytoskeletal organization. Its targeted mechanism of action makes it a valuable molecular tool for dissecting MLCK-dependent signaling pathways in various biological systems, offering researchers a precise approach to study actin-myosin dynamics and related cellular processes.
Signal transduction research: MLCK inhibitor peptide 18 is widely used in studies aiming to elucidate the role of MLCK in intracellular signaling cascades, particularly those governing cytoskeletal rearrangement and contractile events. By specifically blocking MLCK activity, researchers can differentiate between MLCK-dependent and independent pathways, enabling a more nuanced understanding of how external stimuli regulate cell shape, migration, and tension through phosphorylation events. This selective inhibition is instrumental in mapping the downstream effects of calcium-calmodulin signaling and its integration with other regulatory networks.
Cell motility and migration assays: The peptide serves as a critical reagent in experiments investigating the mechanisms of cell movement, including wound healing, chemotaxis, and invasion models. By attenuating MLCK-mediated phosphorylation of myosin light chains, the inhibitor allows scientists to assess the contribution of myosin II contractility to cellular locomotion. Such studies are essential for unraveling the molecular basis of tissue remodeling, embryonic development, and metastasis, where precise control of cell motility is a defining feature.
Endothelial barrier function studies: MLCK activity is a well-established regulator of endothelial permeability, influencing the integrity of vascular barriers through modulation of cytoskeletal tension and cell-cell junctions. MLCK inhibitor peptide 18 is frequently utilized in in vitro models of the endothelium to probe how changes in contractile force affect paracellular permeability. This application supports the investigation of vascular leakage, inflammation, and edema, providing insights into the molecular underpinnings of barrier dysfunction in various physiological and pathological contexts.
Smooth muscle contraction analysis: The peptide is an effective tool for dissecting the contractile mechanisms of smooth muscle tissues in organ bath or cell-based assays. By inhibiting MLCK, researchers can distinguish between MLCK-dependent and alternative pathways driving muscle contraction, such as those involving Rho-associated kinases. This distinction is critical for understanding the regulation of vascular tone, airway reactivity, and gastrointestinal motility, and for identifying new molecular targets in studies of smooth muscle physiology.
Peptide-based inhibitor validation: As a structurally defined synthetic peptide, MLCK inhibitor peptide 18 is also employed as a reference compound in the development and benchmarking of novel MLCK inhibitors. Its well-characterized activity profile allows for comparative studies assessing potency, selectivity, and off-target effects of new molecules. Such validation efforts are fundamental to advancing peptide-based inhibitor design, optimizing structure-activity relationships, and enhancing the specificity of kinase-targeted research tools.
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