SCP0196
Myosin Light Chain Kinase Substrate
≥95% (HPLC), lyophilized
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product name
Myosin Light Chain Kinase Substrate (smooth muscle),
Assay
≥95% (HPLC)
form
lyophilized
composition
Peptide Content, ≥62%
storage condition
protect from light
storage temp.
−20°C
Amino Acid Sequence
Lys-Lys-Arg-Ala-Ala-Arg-Ala-Thr-Ser-Asn-Val-Phe-Ala-NH2
General description
Myosin light chain kinase (MLCK) comprises an N-terminal actin-binding domain, a central kinase domain, and a C-terminal myosin-binding domain.
Application
Myosin Light Chain Kinase Substrate (smooth muscle) has been used in MLCK activity assay to study the role of Plasmodium falciparum calmodulin (Pf CaM).
Biochem/physiol Actions
KKRAARATSNVFA-NH2 is used as a myosin light chain kinase (MLCK) substrate.
Myosin light chain kinase (MLCK) is involved in modulating the actin-myosin interaction of smooth muscle. In addition to its kinase activity, MLCK also has actin-binding activity, which can assemble actin filaments into bundles. It also has myosin-binding activity, which can generate myosin filaments.
Storage Class Code
11 - Combustible Solids
WGK
WGK 3
Flash Point(F)
Not applicable
Flash Point(C)
Not applicable
Certificates of Analysis (COA)
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Gastroenterology, 123(1), 163-172 (2002-07-10)
Maintenance of the mucosal barrier is a critical function of intestinal epithelia. Myosin regulatory light chain (MLC) phosphorylation is a common intermediate in the pathophysiologic regulation of this barrier. The aim of this study was to determine whether a membrane
Bioorganicheskaia khimiia, 36(4), 498-504 (2010-09-09)
Myosin light chain kinase (MLCK) is the key regulator of various forms of cell motility including endothelial and epithelial permeability in particular. One of the potential MLCK inhibitors to be used in humans is a membrane permeable peptide H-RKKYKYRRK-NH2 (L-PIK).
Structure and function of smooth muscle myosin light chain kinase.
Advances in Experimental Medicine and Biology, 453, 229-234 (2019)
Biofizika, 55(6), 1008-1013 (2011-01-28)
The ability of novel cell-permeating peptide molecules derived from the peptide inhibitor of the myosin light chain kinase (MLCK) L-PIK (Arg-Lys-Lys-Tyr-Lys-Tyr-Arg-Arg-Lys) to inhibit this kinase in vitro and attenuate the thrombin-induced hyperpermeability of endothelial cell monolayer in culture has been
Arteriosclerosis, thrombosis, and vascular biology, 25(9), 1831-1836 (2005-07-05)
Rho and its effector Rho-kinase/ROCK mediate cytoskeletal reorganization as well as smooth muscle contraction. Recent studies indicate that Rho and ROCK are critically involved in vascular remodeling. Here, we tested the hypothesis that Rho/ROCK are critically involved in angiotensin II
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