Recombinant Human MLCK Protein

Name: Recombinant Human MLCK Protein
Brand: Beta LifeScience
SKU: BL-0298SG
Availability: InStock

Collections: Other recombinant proteins, Recombinant proteins

Our products are highly customizable to meet your specific needs. You can choose options such as endotoxin removal, liquid or lyophilized forms, preferred tags, and the desired functional sequence range for proteins. Submitting a written inquiry expedites the quoting process.

Submit an inquiry today to inquire about all available size options and prices! Connect with us via the live chat in the bottom corner to receive immediate assistance.

Product Overview

Tag	GST
Host Species	Human
Accession	NM_053025
Synonym	MYLK, KRP, MLCK108, MLCK210, MSTP083, FLJ12216, DKFZp686I10125
Background	MLCK or myosin light chain kinase is a muscle member of the immunoglobulin gene superfamily and is a calcium/calmodulin dependent protein kinase. MLCK is a regulatory protein for smooth muscle contraction, which acts by phosphorylating 20-kDa myosin light chain (MLC20) to activate the myosin ATPase activity. The kinase activity for the phosphorylation is localized at the central part of MLCK, which is also furnished with actin-binding activity at its N terminal and myosin-binding activity at its C terminal (1). Phosphorylation of regulatory light chain of myosin plays an important role in controlling the morphological changes seen during cell division (2).
Description	Recombinant human MLCK (1425-1776) was produced by baculovirus in Sf9 insect cells using a N-terminual GST tag. This protein is purified with our unique purification methods.
Source	Sf9 insect cells
AA Sequence	1425-1776
Molecular Weight	~70 kDa
Purity	For specific purity information on a given lot, see related COA.
Endotoxin	< 1.0 EU per μg of the protein as determined by the LAL method
Bioactivity	Active
Formulation	Recombinant protein is supplied in 50mM Tris-HCl, pH 7.5, 50mM NaCl, 10mM Glutathione, 0.25mM DTT, 0.1mM EDTA, 0.1mM PMSF and 25% glycerol.
Stability	The recombinant protein is stable for up to 12 months at -70°C
Usage	For Research Use Only
Storage	Recombinant Human MLCK Protein should be stored should be stored at < -70°C. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.

Target Details

Target Function	Calcium/calmodulin-dependent myosin light chain kinase implicated in smooth muscle contraction via phosphorylation of myosin light chains (MLC). Also regulates actin-myosin interaction through a non-kinase activity. Phosphorylates PTK2B/PYK2 and myosin light-chains. Involved in the inflammatory response (e.g. apoptosis, vascular permeability, leukocyte diapedesis), cell motility and morphology, airway hyperreactivity and other activities relevant to asthma. Required for tonic airway smooth muscle contraction that is necessary for physiological and asthmatic airway resistance. Necessary for gastrointestinal motility. Implicated in the regulation of endothelial as well as vascular permeability, probably via the regulation of cytoskeletal rearrangements. In the nervous system it has been shown to control the growth initiation of astrocytic processes in culture and to participate in transmitter release at synapses formed between cultured sympathetic ganglion cells. Critical participant in signaling sequences that result in fibroblast apoptosis. Plays a role in the regulation of epithelial cell survival. Required for epithelial wound healing, especially during actomyosin ring contraction during purse-string wound closure. Mediates RhoA-dependent membrane blebbing. Triggers TRPC5 channel activity in a calcium-dependent signaling, by inducing its subcellular localization at the plasma membrane. Promotes cell migration (including tumor cells) and tumor metastasis. PTK2B/PYK2 activation by phosphorylation mediates ITGB2 activation and is thus essential to trigger neutrophil transmigration during acute lung injury (ALI). May regulate optic nerve head astrocyte migration. Probably involved in mitotic cytoskeletal regulation. Regulates tight junction probably by modulating ZO-1 exchange in the perijunctional actomyosin ring. Mediates burn-induced microvascular barrier injury; triggers endothelial contraction in the development of microvascular hyperpermeability by phosphorylating MLC. Essential for intestinal barrier dysfunction. Mediates Giardia spp.-mediated reduced epithelial barrier function during giardiasis intestinal infection via reorganization of cytoskeletal F-actin and tight junctional ZO-1. Necessary for hypotonicity-induced Ca(2+) entry and subsequent activation of volume-sensitive organic osmolyte/anion channels (VSOAC) in cervical cancer cells. Responsible for high proliferative ability of breast cancer cells through anti-apoptosis.
Subcellular Location	Cytoplasm. Cell projection, lamellipodium. Cleavage furrow. Cytoplasm, cytoskeleton, stress fiber.
Protein Families	Protein kinase superfamily, CAMK Ser/Thr protein kinase family
Database References	HGNC: 7590 OMIM: 600922 KEGG: hsa:4638 STRING: 9606.ENSP00000353452 UniGene: Hs.477375
Associated Diseases	Aortic aneurysm, familial thoracic 7 (AAT7)
Tissue Specificity	Smooth muscle and non-muscle isozymes are expressed in a wide variety of adult and fetal tissues and in cultured endothelium with qualitative expression appearing to be neither tissue- nor development-specific. Non-muscle isoform 2 is the dominant splice

Gene Functions References

miR155 directly suppressed the expression of MYLK without affecting the RhoA pathway. PMID: 29901087
the MAPKspecific inhibitor SB203580 attenuated the inhibitory effects of 4HPR on the migration of HepG2 cells. Moreover, we also observed that 4HPR inhibited the activation and expression of myosin light chain kinase (MLCK) in HepG2 cells. PMID: 29767236
Recombinant human MLCK was concentration- and time-dependently degraded by recombinant human MMP9 in vitro, and this process was prevented by the MMP9 inhibitor. PMID: 29262413
High expression of MLCK is correlated with metastatic triple negative breast cancer. PMID: 27563827
Interaction between kinase domain and regulatory light chain (RLC) substrate is identified in the absence of calmodulin, indicating restored substrate-binding capability due to mechanically induced removal of the auto-inhibitory regulatory region. PMID: 28696205
loss of MLCK contributes to the migratory properties of epithelial cells resulting from changes in cell-cell and cell-matrix adhesions, and increased epidermal growth factor receptor signaling. PMID: 26876209
Its phosphorylation and dephosphorylation regulate smooth muscle contraction and relaxation. PMID: 27375035
Sixty-seven experienced runners competed in a marathon race. The MLCK genotype (C37885A) of these marathoners was determined. CA heterozygotes for MLCK C37885A might present higher exercise-induced muscle damage after a marathon competition than CC counterparts. PMID: 27483374
three Megacystis microcolon intestinal hypoperistalsis syndrome (MMHS)-affected subjects from two consanguineous families with no variants in the known MMIHS-associated genes. PMID: 28602422
these Acute respiratory distress syndrome (ARDS)-associated MYLK cytosine-guanine dinucleotides with effect modification by ethnicity and local modified cytosine quantitative trait loci suggest that MYLK epigenetic variation and local genetic background may contribute to health disparities observed in ARDS. PMID: 27543902
mechanical stress and MYLK single nucleotide polymorphism regulate MYLK alternative splicing. PMID: 27529643
Rebeccamycin attenuates TNF-alpha-induced disruption of intestinal epithelial barrier integrity by inducing claudin-5 expression and suppressing MLCK production via Chk1 activation. PMID: 28391269
Data show that alterations in myosin light chain kinase activity, claudin-15 and claudin-2 expression are associated with gluten-induced symptomatology and intestinal permeability changes in diarrhea-predominant irritable bowel syndrome (IBS-D). PMID: 27869798
PXR regulates the intestinal epithelial barrier during inflammation by modulating cytokine-induced MLCK expression and JNK1/2 activation PMID: 27440420
A 2-bp deletion in myosin light chain kinase (c3272_3273del, p.Ser1091*) that led to a premature stop codon have a high risk of presenting with an acute aortic dissection or rupture. PMID: 27586135
In contrast to mylk2 and mylk3, mylk1 has a complex structure, and multiple protein products of the mylk1 gene are expressed in most if not all cell types. This review deals with the mylk1 gene and its protein products- multiple MLCK isoforms and noncatalytic KRP/telokin protein. [Review] PMID: 28260490
Likely pathogenic variants included a TGFB2 variant in one patient and a SMAD3 variant in another. These variants have been reported previously in individuals with similar phenotypes. Variants of uncertain significance of particular interest included novel variants in MYLK and MFAP5, which were identified in a third patient PMID: 26854089
suggest a novel role for myosin light chain and myosin light chain kinase in advanced glycation end product-induced endothelial hyperpermeability PMID: 26607798
TKS5 and MYLK represent two mediators of invasive behavior of cancer cells that are regulated by the ZEB1/miR-200 feedback loop PMID: 26334100
We speculate that the drop of the ROCK-to-MLCK ratio may occur as an attempt to compensate for the increased Rho kinase activity. PMID: 26468005
study demonstrates that G. duodenalis-mediated disruption of villin is, at least, in part dependent on activation of myosin light chain kinase (MLCK). PMID: 26334299
Gene-based association analyses shows nominal significant association with multifocal fibromuscular dysplasia for myosin light chain kinase. PMID: 26147384
These structure-function studies suggest novel mechanisms for nmMLCK regulation, which may confirm MYLK as a candidate gene in inflammatory lung disease and advance knowledge of the genetic underpinning of lung-related health disparities. PMID: 26111161
nmMLCK variant (721C) mRNA secondary structure exhibits increased stability and greater efficiency in protein translation initiation. PMID: 25271083
inhibition of p38 MAP kinase attenuated the histamine response in all three EC types. Inhibition of RhoA, ROCK, or MLCK also prevented the histamine-induced decrease in TER in HDMEC. PMID: 25582918
Fine mapping of the myosin light chain kinase (MYLK) gene replicates the association with asthma in populations of Spanish descent. PMID: 26025125
serum MLCK is associated with Type 2 diabetes mellitus. PMID: 25696011
Data suggest that expression of MLCK, myosin light chain, and myosin heavy chain 11 (MYH11) is up-regulated in uterine myoma as compared to adjacent smooth muscle cells; phosphorylation/activation of MLCK appears to be involved in cell proliferation. PMID: 25181625
The Smooth muscle myosin light chain kinase (MLCK) contributes to Ca(2+) flux regulation in vascular smooth muscle (VSM) and in non-muscle cells, where cytoskeleton has been suggested to help Ca(2+) channels trafficking. PMID: 25483583
Melatonin protects the esophageal epithelial barrier by suppressing the transcription, translation and activity of MLCK through ERK1/2 signal transduction PMID: 25562159
epithelial MLCK-activated brush border fanning by IFN-gamma promotes adherence and internalization of normally noninvasive enteric bacteria PMID: 24911373
These findings suggested that low MYLK and MYL9 expressions might be associated with the development of NSCLC. PMID: 25179839
IgE has a role in regulating smMLCK in HASM cells PMID: 24722483
Increased human lung endothelial cell expression of MYLK by bioactive agonists (excessive mechanical stress, TNF-alpha) is regulated in part by specific miRNAs (miR-374a, miR-374b, miR-520c-3p, and miR-1290). PMID: 23492194
Claudin-2 assumes an important role in colorectal inflammation, and furthermore implicates the involvement of MLCK in colon inflammation. PMID: 23306855
these studies show that the IL-1beta-induced increase in intestinal tight junction permeability was regulated by p38 kinase activation of ATF-2 and by ATF-2 regulation of MLCK gene activity PMID: 23656735
The approximate time period of changes in the ratios of MLCK-108 and MLCK-210 was revealed (between 8-9 and 13 weeks), that can be associated with functional changes in the developing myocardium. PMID: 22808459
MYLK SNPs downregulate smooth muscle MLCK promoter activity due to interruption of a FOXN1 binding site. These data provide new insights into the contribution of MYLK SNPs to inflammatory disease susceptibility. PMID: 22015949
MLCK is essential for the translocation and association of cortactin and p47phox. PMID: 22219181
Hypermethylated FAM5C and MYLK in serum are strongly associated with the development of gastric cancer and can be used as potential biomarkers for diagnosis and pre-warning. PMID: 22377736
IL-18 may potentiate inflammation in the context of inflammatory bowel disease by facilitating neutrophil transepithelial migration via MLCK-dependent disruption of tight junctional occludin. PMID: 22135309
Results provide evidence that neutrophil transmigration is regulated by myosin light chain kinase-mediated endothelial cell contraction and that this event depends on subendothelial cell matrix stiffness. PMID: 21652678
MLCK inhibits the restoration of GPIbalpha in PAR1 pathway during the course of thrombin receptor activation in platelets. PMID: 19549383
No association between snps in the myosin light chain kinase gene and either the need for positive-pressure ventilation or the development of acute lung injury/acute respiratory distress syndrome was observed in children with community-acquired pneumonia. PMID: 20081554
Studies indicate an essential role for Abl kinase in vascular barrier regulation via posttranslational modification of nmMLCK. PMID: 20861316
genetic and functional studies support the conclusion that heterozygous loss-of-function mutations in MYLK are associated with aortic dissections. PMID: 21055718
Data provide insights into the molecular basis for vascular barrier-regulatory cytoskeletal responses and quantified the critical interactions between non-muscle MLCK isoenzymes and cortactin during vascular barrier regulation. PMID: 20053363
study concludes MLCK is responsible for high proliferative ability of breast cancer cells through anti-apoptosis, in which p38 pathway was involved PMID: 20453870
membrane blebbing in response to AT(1)R signaling is dependent on beta-arrestin2 and is mediated by a RhoA/ROCK/MLCK-dependent pathway PMID: 20181817
hARD1 is a bona fide regulator of MLCK, and hARD1 plays a crucial role in the balance between tumor cell migration and stasis PMID: 19826488

FAQs

Please fill out the Online Inquiry form located on the product page. Key product information has been pre-populated. You may also email your questions and inquiry requests to sales1@betalifesci.com. We will do our best to get back to you within 4 business hours.

Feel free to use the Chat function to initiate a live chat. Our customer representative can provide you with a quote immediately.

Proteins are sensitive to heat, and freeze-drying can preserve the activity of the majority of proteins. It improves protein stability, extends storage time, and reduces shipping costs. However, freeze-drying can also lead to the loss of the active portion of the protein and cause aggregation and denaturation issues. Nonetheless, these adverse effects can be minimized by incorporating protective agents such as stabilizers, additives, and excipients, and by carefully controlling various lyophilization conditions.

Commonly used protectant include saccharides, polyols, polymers, surfactants, some proteins and amino acids etc. We usually add 8% (mass ratio by volume) of trehalose and mannitol as lyoprotectant. Trehalose can significantly prevent the alter of the protein secondary structure, the extension and aggregation of proteins during freeze-drying process; mannitol is also a universal applied protectant and fillers, which can reduce the aggregation of certain proteins after lyophilization.

Our protein products do not contain carrier protein or other additives (such as bovine serum albumin (BSA), human serum albumin (HSA) and sucrose, etc., and when lyophilized with the solution with the lowest salt content, they often cannot form A white grid structure, but a small amount of protein is deposited in the tube during the freeze-drying process, forming a thin or invisible transparent protein layer.

Reminder: Before opening the tube cap, we recommend that you quickly centrifuge for 20-30 seconds in a small centrifuge, so that the protein attached to the tube cap or the tube wall can be aggregated at the bottom of the tube. Our quality control procedures ensure that each tube contains the correct amount of protein, and although sometimes you can't see the protein powder, the amount of protein in the tube is still very precise.

To learn more about how to properly dissolve the lyophilized recombinant protein, please visit Lyophilization FAQs.