Analytical Data
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Gene name
MYH7
- Application
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Alternative Names
MYH7；KIAA1512；Myosin-7B
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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
P12883
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Expression Region
1-109aa
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AA Sequence
MGDSEMAVFGAAAPYLRKSEKERLEAQTRPFDLKKDVFVPDDKQEFVKAKIVSREGGKVTAETEYGKTVTVKEDQVMQQNPPKFDKIEDMAMLTFLHEPAVLYNLKDRY
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Molecular Weight
18.1 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
MYH7, also known as beta-myosin heavy chain, is a critical component of the thick filament in cardiac and skeletal muscle cells, playing a crucial role in muscle contraction and function. Mutations in the MYH7 gene are associated with various cardiac diseases, particularly familial hypertrophic cardiomyopathy (FHC), which can lead to heart failure and sudden cardiac death. Research on MYH7 recombinant proteins is essential for understanding the structural and functional implications of these mutations, as well as developing targeted therapies. By producing and characterizing MYH7 recombinant proteins, scientists can investigate the molecular mechanisms underlying muscle contraction and elucidate how specific genetic alterations affect protein stability, assembly, and function. This research not only advances our knowledge of cardiac physiology but also holds potential for innovative therapeutic strategies to manage MYH7-related pathologies. Moreover, the study of MYH7 recombinant proteins can facilitate drug screening processes and aid in the development of precision medicine approaches for patients with hereditary cardiovascular disorders. As such, the exploration of MYH7 protein dynamics remains a vital area of investigation in both basic research and clinical applications.
