Analytical Data
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Gene name
DDX27
- Application
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Alternative Names
DEAD box protein 27
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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
Q96GQ7
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Expression Region
30-794aa
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Molecular Weight
102.5 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
Related Products
Protein Description
DDX27, a member of the DEAD-box RNA helicase family, is implicated in various cellular processes, including RNA metabolism, ribosome biogenesis, and gene expression regulation. Its role in modulating transcription and RNA processing highlights its potential significance in cellular stress responses and developmental processes. Recent studies suggest that DDX27 may be involved in various diseases, including cancers, due to its influence on cell proliferation and apoptosis. Given the increasing recognition of RNA helicases as pivotal regulators in cellular homeostasis and disease, the recombinant production of DDX27 serves as a crucial step for understanding its structure-function relationships and biological roles. By generating DDX27 in a recombinant form, researchers can perform in-depth biochemical and biophysical analyses, elucidating its mechanistic pathways and interactions with RNA and other protein partners. This knowledge is essential for assessing its potential as a therapeutic target, especially in oncological contexts where dysregulation of RNA processing is prevalent. Thus, the research surrounding DDX27 recombinant proteins not only advances our understanding of fundamental biological processes but also opens avenues for the development of novel therapeutic strategies.
