Analytical Data
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Gene name
MYH10
- Application
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Alternative Names
NMMHCB; Cellular myosin heavy chain, type B; Myosin heavy chain, non-muscle IIb
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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 90% as determined by SDS-PAGE.
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Uniprot
P35580
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Expression Region
Thr438~Lys716
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Molecular Weight
33kDa
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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
MYH10, a gene encoding a non-muscle myosin II heavy chain, plays a crucial role in various cellular processes, including cell motility, division, and mechanotransduction. Abnormal expression or mutations in MYH10 have been linked to several pathological conditions, such as cancer metastasis and cardiovascular diseases. The study of MYH10 recombinant protein has garnered attention due to its potential applications in understanding the molecular mechanisms underlying these diseases. Researchers aim to produce MYH10 in a recombinant form to facilitate detailed investigations of its structural and functional properties. This includes studying its interaction with other cytoskeletal proteins and its role in actin filament dynamics. By utilizing advanced techniques such as crystallography and cryo-electron microscopy, scientists can gain insights into the conformational changes that MYH10 undergoes during its function in the cellular context. Moreover, the recombinant MYH10 protein serves as a valuable tool for screening potential therapeutic agents that could modulate its activity or expression, thereby providing new avenues for targeted treatments in diseases associated with dysregulated myosin function. Overall, the exploration of MYH10 recombinant protein not only enhances our understanding of fundamental cellular mechanisms but also opens up possibilities for novel therapeutic strategies.
