Analytical Data
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Gene name
MYL9
- Application
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Alternative Names
MLC2; LC20; MYRL2; MRLC1; 20 kDa myosin light chain; Myosin Regulatory Light Chain 2,Smooth Muscle Isoform; Myosin Regulatory Light Chain 1
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Species
Human
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Source
E. coli
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Tag
N-His
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Purity
Greater than 95% as determined by SDS-PAGE.
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Uniprot
P24844
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Expression Region
Arg5~Leu163
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Molecular Weight
20kDa
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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
Related Products
Protein Description
MYL9, or myosin light chain 9, is a critical protein that plays a vital role in various cellular functions, including muscle contraction, cell motility, and cytokinesis. It is a key component of the myosin-2 motor protein complex, which is essential for the actin-myosin interaction that drives muscle contraction and other cellular movements. Given its significant involvement in cellular mechanics, MYL9 has garnered attention in biomedical research, particularly regarding cardiac and skeletal muscle development, as well as in the study of diseases such as cancer and heart failure. The study of MYL9 has revealed that its phosphorylation status can regulate various cellular processes, influencing cell shape, adhesion, and migration. Researchers have increasingly focused on the development of recombinant MYL9 protein to better understand its functional properties and regulatory mechanisms. Recombinant MYL9 can be used in numerous applications, including structural studies, drug screening, and as a potential therapeutic target. Advancements in recombinant protein technology have enabled the production of MYL9 with enhanced purity and activity, facilitating deeper insights into its biological roles. This ongoing research aims to elucidate the precise mechanisms by which MYL9 contributes to cellular dynamics and its implications in health and disease, providing a foundation for potential therapeutic interventions.
