Recombinant Human Myosin Light Chain Kinase, Smooth Muscle (MYLK) Protein (His)

Name: Recombinant Human Myosin Light Chain Kinase, Smooth Muscle (MYLK) Protein (His)
Brand: Beta LifeScience
SKU: BLC-01886P
Availability: InStock

Greater than 85% as determined by SDS-PAGE.

Collections: All products, High-quality recombinant proteins, Other recombinant proteins

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Product Overview

Description	Recombinant Human Myosin Light Chain Kinase, Smooth Muscle (MYLK) Protein (His) is produced by our E.coli expression system. This is a protein fragment.
Purity	Greater than 85% as determined by SDS-PAGE.
Uniprotkb	Q15746
Target Symbol	MYLK
Synonyms	Kinase-related protein
Species	Homo sapiens (Human)
Expression System	E.coli
Tag	N-10His
Target Protein Sequence	YDIEERLGSGKFGQVFRLVEKKTRKVWAGKFFKAYSAKEKENIRQEISIMNCLHHPKLVQCVDAFEEKANIVMVLEIVSGGELFERIIDEDFELTERECIKYMRQISEGVEYIHKQGIVHLDLKPENIMCVNKTGTRIKLIDFGLARRLENAGSLKVLFGTPEFVAPEVINYEPIGYATDMWSIGVICYILVSGLSPFMGDNDNETLANVTSATWDFDDEAFDEISDDAKDFISNLLKKDMKNRLDCTQCLQHPWL
Expression Range	1464-1719aa
Protein Length	Partial
Mol. Weight	35.4 kDa
Research Area	Signal Transduction
Form	Liquid or Lyophilized powder
Buffer	Liquid form: default storage buffer is Tris/PBS-based buffer, 5%-50% glycerol. Lyophilized powder form: the buffer before lyophilization is Tris/PBS-based buffer, 6% Trehalose, pH 8.0.
Reconstitution	Briefly centrifuged the vial prior to opening to bring the contents to the bottom. Reconstitute protein in deionized sterile water to a concentration of 0.1-1.0 mg/mL. It is recommended to add 5-50% of glycerol (final concentration) and aliquot for long-term storage at -20°C/-80°C. The default final concentration of glycerol is 50%.
Storage	1. Store at -20°C/-80°C upon receipt, aliquoting is necessary for mutiple use. 2. Avoid repeated freeze-thaw cycles. 3. Store working aliquots at 4°C for up to one week. 4. In general, protein in liquid form is stable for up to 6 months at -20°C/-80°C. Protein in lyophilized powder form is stable for up to 12 months at -20°C/-80°C.
Notes	Repeated freezing and thawing is not recommended. Store working aliquots at 4°C for up to one week.

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: 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

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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.

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