Analytical Data
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Gene name
Des
- Application
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Alternative Names
CMD1I; CSM1; CSM2; Intermediate Filament Protein
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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
P17661
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Expression Region
Asp117~Gln348
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Molecular Weight
29kDa
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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
Desmin is a type of intermediate filament protein that plays a crucial role in maintaining the structural integrity and function of skeletal and cardiac muscle cells. Research on desmin has gained significant attention due to its involvement in various myopathies and cardiomyopathies. Mutations in the desmin gene can lead to muscle dysfunction, progressive weakness, and heart failure. The understanding of desmin's role at the molecular level has important implications for developing therapeutic strategies for related diseases. Scientists have employed various biochemical and genetic approaches to study desmin's structure, assembly, and interactions with other cellular components. Recent advancements in techniques such as cryo-electron microscopy and advanced imaging have provided deeper insights into its organization within the muscle fibers. Additionally, studies have explored the potential of desmin as a biomarker for disease progression and therapeutic targets. Understanding the mechanisms underlying desmin-related disorders not only sheds light on muscle cell biology but also paves the way for innovative treatments aimed at enhancing muscle health and cardiac function.
