Analytical Data
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Gene name
MLCK
- Application
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Alternative Names
zgc:92755; atrial isoform; cmlc2; MGC92755; MLC-2a; MLC2a; MLCK; cardiac; MLRA_HUMAN; MYL2A; MYL7; Mylc2a; Myosin light chain 2a; Myosin light chain 7 regulatory; Myosin light polypeptide 7 regulatory; Myosin regulatory light chain 2; Myosin regulatory light chain 2 atrial isoform; Myosin regulatory light chain 7
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Species
Human
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Source
E. coli
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Tag
His tag N-Terminus
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
Q01449
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Expression Region
1-175 aa
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AA Sequence
MASRKAGTRGKVAATKQAQRGSSNVFSMFEQAQIQEFKEAFSCIDQNRDGIICKADLRETYSQLGKVSVPEEELDAMLQEGKGPINFTVFLTLFGEKLNGTDPEEAILSAFRMFDPSGKGVVNKDEFKQLLLTQADKFSPAEVEQMFALTPMDLAGNIDYKSLCYIITHGDEKEE
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Molecular Weight
46.4 kDa
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Endotoxin
< 1.0 EU per μg protein as determined by the LAL method.
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Form
Freeze-dried powder
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Buffer formulation
PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300.
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Reconstitution
Reconstitute in ddH2O to a concentration of 0.1-0.5 mg/mL. Do not vortex.
- Customization
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Stability Test
The thermal stability is described by the loss rate. The loss rate was determined by accelerated thermal degradation test, that is, incubate the protein at 37℃ for 48h, and no obvious degradation and precipitation were observed. The loss rate isless than 8% within the expiration date under appropriate storage condition.
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Storage & Shelf Life
Samples are stable for up to twelve months from date of receipt at -20℃ to -80℃. Store it under sterile conditions at -20℃ to -80℃. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.
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Shipping
In general, recombinant proteins are supplied as lyophilized powder and shipped at ambient temperature. For bulk packages, the proteins are provided as frozen liquid and shipped with blue ice, unless otherwise requested by the customer.
Quality inspection process
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Protein Description
Myosin light chain kinase (MLCK) is a crucial enzyme that plays a significant role in cellular processes, particularly in muscle contraction and various signaling pathways. It phosphorylates the myosin light chain, which is essential for muscle contraction in both smooth and striated muscles, thereby regulating smooth muscle contraction and influencing cellular functions such as motility and contraction in non-muscle cells. The understanding of MLCK’s structure and function has important implications in various physiological and pathological conditions, including cardiovascular diseases, asthma, and cancer. Research on MLCK recombinant proteins has gained momentum as scientists strive to elucidate the intricate details of its mechanism of action, post-translational modifications, and interactions with various cellular partners. By producing and purifying MLCK as a recombinant protein, researchers aim to perform in-depth biochemical studies that can shed light on its regulatory mechanisms and potential therapeutic targets. Moreover, studies on MLCK variants and their effects on muscle function can provide insights into the development of muscle-related diseases and pave the way for novel interventions. Overall, the investigation of MLCK through recombinant protein technology is a promising avenue for developing a deeper understanding of its biological roles and therapeutic potential in various diseases.











