Analytical Data
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Gene name
DDX5
- Application
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Alternative Names
DEAD box protein 5 (RNA helicase p68 G17P1) (HELR) (HLR1)
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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
P17844
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Expression Region
1-614aa
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Molecular Weight
74.1 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
DDX5, also known as DEAD-box helicase 5, is an RNA helicase that plays a crucial role in various cellular processes, including RNA metabolism, transcription regulation, and ribosome biogenesis. It is part of the DEAD-box protein family, characterized by the presence of a highly conserved DEAD motif, which is implicated in ATP-dependent RNA unwinding. Research has shown that DDX5 is involved in the regulation of gene expression and has been linked to several biological processes such as cell proliferation, differentiation, and apoptosis. Its dysregulation has been implicated in various diseases, including cancer, where it can affect the expression of oncogenes and tumor suppressor genes. The study of DDX5 recombinant protein is essential for understanding its functional mechanisms and interactions with RNA and other proteins. By producing DDX5 as a recombinant protein, researchers can analyze its enzymatic activity, binding affinity, and role in RNA-related processes in vitro. This research has potential therapeutic implications, as targeting DDX5 could provide new strategies for treating diseases where its function is altered. Additionally, understanding the structural and functional properties of DDX5 can shed light on the intricate networks of RNA regulation in cells, further underscoring the importance of this helicase in cellular homeostasis and disease development.
