Analytical Data
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Gene name
MYO19
- Application
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Alternative Names
Myosin head domain-containing protein 1
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Species
Human
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Source
E. coli
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Tag
N- His-SUMO
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
Q96H55
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Expression Region
2-770aa
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Molecular Weight
102.6 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
MYO19 is a member of the myosin superfamily, which plays a critical role in various cellular processes, including organelle transport and cell motility. Recent studies have highlighted its essential function in the mitochondrial dynamics and distribution within cells, suggesting that MYO19 is involved in the maintenance of mitochondrial health and function. The protein is particularly interesting because mutations or dysregulation in MYO19 have been correlated with several pathological conditions, including neurodegenerative diseases and metabolic disorders. Given its significance in cellular energy homeostasis, researchers are increasingly focused on characterizing MYO19 through recombinant protein techniques. This approach allows for in-depth analysis of MYO19's structure, function, and interactions with other cellular components. Understanding MYO19 at the molecular level is not only critical for elucidating its biological roles but also holds potential for developing therapeutic strategies to combat diseases associated with mitochondrial dysfunction. Hence, the study of recombinant MYO19 protein is gaining momentum in both fundamental and applied biological research, paving the way for discoveries that could lead to novel interventions in mitochondrial-related diseases.
