Analytical Data
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Gene name
DDX1
- Application
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Alternative Names
(DEAD box protein 1)(DEAD box protein retinoblastoma)(DBP-RB)
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Species
Human
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Source
E. coli
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Tag
N- His & C- Myc
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
Q92499
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Expression Region
1-740aa
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Molecular Weight
89.9 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
DDX1, a member of the DEAD-box RNA helicase family, plays a crucial role in various cellular processes, including RNA metabolism, splicing, and translation. Its significance has been underscored in several studies linking DDX1 to cancer biology, viral infections, and immune responses. Dysregulation of DDX1 expression has been associated with tumorigenesis, highlighting its potential as a biomarker for cancer prognosis. Recent advancements in recombinant protein technology have enabled the production of DDX1 in significant quantities, facilitating in-depth studies on its structure-function relationship and interaction with RNA substrates. Furthermore, understanding the mechanistic roles of DDX1 could provide insights into therapeutic strategies targeting RNA processing pathways. Researchers are now focusing on characterizing the biochemical properties of recombinant DDX1, including its helicase activity and affinity for various RNA sequences, which may lead to novel approaches in cancer treatment and antiviral therapies. The development of DDX1 as a recombinant protein not only opens avenues for basic research but also enhances our understanding of its regulatory mechanisms, reinforcing its importance in cellular homeostasis and disease contexts. Overall, the study of DDX1 as a recombinant protein is pivotal for elucidating its broader implications in molecular biology and therapeutic applications.
