Analytical Data
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Gene name
MYH2
- Application
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Alternative Names
MYH2；MYHSA2；Myosin-2
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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
Q9UKX2
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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
MYH2, a member of the myosin heavy chain gene family, plays a crucial role in muscle contraction and has been implicated in various myopathies. Research on MYH2 recombinant proteins has gained significant attention due to the gene's association with congenital muscle disorders, particularly those affecting skeletal muscle tissues. Mutations in the MYH2 gene can lead to phenotypes characterized by weakness and muscle fiber type abnormalities. Understanding the structure and function of MYH2 is essential for elucidating its role in muscle physiology and pathology. Scientists use recombinant protein techniques to produce MYH2 in model systems, allowing for detailed studies on its biochemical properties, interactions with other muscle proteins, and the effects of specific mutations. This research not only aids in deciphering the molecular underpinnings of MYH2-related diseases but also paves the way for potential therapeutic strategies, including gene therapy and targeted treatments aimed at restoring normal muscle function. Through these studies, significant insights into muscle biology and the broader framework of muscle-related conditions can be achieved, fostering advancements in clinical approaches to manage myopathies linked to MYH2.
