Recombinant human Myosin light chain kinase/MLCK protein
Be the first to review this product! Submit a review
|
(1 Publication)
Recombinant human Myosin light chain kinase/MLCK protein is a Human Fragment protein, in the 1425 to 1776 aa range, expressed in Insect cells, with >95%, suitable for SDS-PAGE, FuncS.
View Alternative Names
MLCK, MLCK1, MYLK1, MYLK, smMLCK, Kinase-related protein, Telokin, KRP
- FuncS
Unknown
Functional Studies - Recombinant human Myosin light chain kinase/MLCK protein (AB55674)
The specific activity of Myosin light chain kinase/MLCK (ab55674) was determined to be 180 nmol/min/mg as per activity assay protocol
- SDS-PAGE
Unknown
SDS-PAGE - Recombinant human Myosin light chain kinase/MLCK protein (AB55674)
- SDS-PAGE
Unknown
SDS-PAGE - Recombinant human Myosin light chain kinase/MLCK protein (AB55674)
SDS PAGE analysis of ab55674
Reactivity data
Product details
ab60014 (Mouse MYL9 full length protein) can be utilized as a substrate for assessing Kinase activity
Previously labelled as Myosin light chain kinase.
Sequence info
Properties and storage information
Shipped at conditions
Appropriate short-term storage conditions
Appropriate long-term storage conditions
Aliquoting information
Storage information
Supplementary information
This supplementary information is collated from multiple sources and compiled automatically.
Biological function summary
Myosin light chain kinase plays a critical role in the regulation of muscle contraction and cellular motility. By phosphorylating the myosin light chain MLCK allows the interaction of actin and myosin which is essential for muscle contraction and movement. In smooth muscle MLCK activity is important for regulating vascular tone and blood pressure. As part of a complex with calmodulin MLCK activation depends on calcium levels linking its activity with intracellular signaling pathways influenced by calcium ions.
Pathways
Myosin light chain kinase is an integral part of the calcium-calmodulin pathway where it acts in response to increased intracellular calcium levels signaled through various cellular activities. This kinase is also involved in the RhoA-Rho kinase pathway which regulates smooth muscle contraction and cytoskeletal dynamics. Related proteins in these pathways include calmodulin whose binding activates MLCK and RhoA a small GTPase associated with the assembly of actin-myosin filaments.
Specifications
Form
Liquid
Additional notes
Affinity purified.
General info
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.
Sequence similarities
Belongs to the protein kinase superfamily. CAMK Ser/Thr protein kinase family.
Post-translational modifications
Can probably be down-regulated by phosphorylation. Tyrosine phosphorylation by ABL1 increases kinase activity, reverses MLCK-mediated inhibition of Arp2/3-mediated actin polymerization, and enhances CTTN-binding. Phosphorylation by SRC at Tyr-464 and Tyr-471 promotes CTTN binding.. The C-terminus is deglutamylated by AGTPBP1/CCP1, AGBL1/CCP4 and AGBL4/CCP6, leading to the formation of Myosin light chain kinase, smooth muscle, deglutamylated form. The consequences of C-terminal deglutamylation are unknown (By similarity).. Acetylated at Lys-608 by NAA10/ARD1 via a calcium-dependent signaling; this acetylation represses kinase activity and reduces tumor cell migration.
Target data
Publications (1)
Recent publications for all applications. Explore the full list and refine your search
iScience 25:104484 PubMed35720262
2022
Applications
Unspecified application
Species
Unspecified reactive species
Product promise
Please note: All products are 'FOR RESEARCH USE ONLY. NOT FOR USE IN DIAGNOSTIC OR THERAPEUTIC PROCEDURES'.
For licensing inquiries, please contact partnerships@abcam.com