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AB55674

Recombinant human Myosin light chain kinase/MLCK protein

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(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

3 Images
Functional Studies - Recombinant human Myosin light chain kinase/MLCK protein (AB55674)
  • 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 - 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 - 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

Key facts

Purity

>95% Densitometry

Expression system

Insect cells

Tags

GST tag N-Terminus

Applications

SDS-PAGE, FuncS

applications

Biologically active

Yes

Biological activity

Specific Activity: 200nm/min/mg.

Accession

Q15746

Animal free

No

Carrier free

No

Species

Human

Storage buffer

pH: 7.5 Constituents: 25% Glycerol (glycerin, glycerine), 0.87% Sodium chloride, 0.79% Tris HCl, 0.00385% (R*,R*)-1,4-Dimercaptobutan-2,3-diol, 0.0038% EGTA, 0.00292% EDTA, 0.00174% PMSF

storage-buffer

Reactivity data

{ "title": "Reactivity Data", "filters": { "stats": ["", "Reactivity", "Dilution Info", "Notes"] }, "values": { "SDS-PAGE": { "reactivity":"TESTED_AND_REACTS", "dilution-info":"", "notes":"<p></p>" }, "FuncS": { "reactivity":"TESTED_AND_REACTS", "dilution-info":"", "notes":"<p></p>" } } }

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

[{"sequence":"","proteinLength":"Fragment","predictedMolecularWeight":null,"actualMolecularWeight":null,"aminoAcidEnd":1776,"aminoAcidStart":1425,"nature":"Recombinant","expressionSystem":null,"accessionNumber":"Q15746","tags":[{"tag":"GST","terminus":"N-Terminus"}]}]

Properties and storage information

Shipped at conditions
Dry Ice
Appropriate short-term storage conditions
-80°C
Appropriate long-term storage conditions
-80°C
Aliquoting information
Upon delivery aliquot
Storage information
Avoid freeze / thaw cycle
True

Supplementary information

This supplementary information is collated from multiple sources and compiled automatically.

Myosin light chain kinase also known as MLCK is an enzyme that phosphorylates myosin light chain proteins facilitating muscle contraction. This kinase primarily interacts with myosin a molecular motor protein responsible for converting chemical energy into mechanical force. The myosin light chains are a part of this complex and are important for regulating myosin's ATPase activity. The molecular weight of MLCK is approximately 130 kDa. It is expressed in various tissues including smooth muscle skeletal muscle and endothelial cells reflecting its central role in these muscle types.
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.

Myosin light chain kinase has links to cardiovascular diseases such as hypertension due to its role in smooth muscle contraction and blood vessel function. Asthma is another condition related to MLCK as the kinase influences airway smooth muscle tone which can affect breathing. Dysregulation of MLCK activity can manifest in altered muscle contractility in these diseases making it a potential target for therapeutic intervention. Research continues to explore the kinase's interactions with calmodulin and other proteins within these disease pathways.

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.

Product protocols

Target data

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.
See full target information MYLK

Publications (1)

Recent publications for all applications. Explore the full list and refine your search

iScience 25:104484 PubMed35720262

2022

Distinct actin-tropomyosin cofilament populations drive the functional diversification of cytoskeletal myosin motor complexes.

Applications

Unspecified application

Species

Unspecified reactive species

Theresia Reindl,Sven Giese,Johannes N Greve,Patrick Y Reinke,Igor Chizhov,Sharissa L Latham,Daniel P Mulvihill,Manuel H Taft,Dietmar J Manstein
View all publications

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