Analytical Data
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Gene name
MYH1
- Application
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Alternative Names
MYH1；Myosin-1
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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
P12882
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Expression Region
全长
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AA Sequence
full
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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
MYH1, or myosin heavy chain 1, is critically involved in muscle contraction and is predominantly expressed in skeletal muscle tissues. Research into MYH1 recombinant protein has gained significance due to its role in various muscle-related diseases and conditions. Mutations in the MYH1 gene can lead to myopathies, muscle weakness, and other muscle dysfunctions. By studying MYH1 recombinant proteins, researchers aim to understand the molecular mechanisms underlying muscle contraction and the pathophysiology of related disorders. The production of MYH1 as a recombinant protein allows for extensive biochemical and biophysical analyses, providing insights into its structure-function relationships. Additionally, the availability of MYH1 recombinant protein can facilitate the development of therapeutic strategies, such as gene therapy or protein replacement, for conditions caused by MYH1 deficiencies. Understanding the dynamics of MYH1 in muscle physiology and pathology can also aid in the advancement of regenerative medicine and muscle rehabilitation techniques. Overall, research on MYH1 recombinant protein not only enhances our fundamental knowledge of muscle biology but also holds potential for practical applications in treating muscle disorders.
