Analytical Data
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Gene name
Dbil5
- Application
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Alternative Names
Endozepine-like peptide
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Species
Mouse
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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
O09035
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Expression Region
1-87aa
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Molecular Weight
13.9 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
Related Products
Protein Description
Dbil5, a member of the DExH/D box family of ATP-dependent RNA helicases, has garnered significant interest in recent years due to its pivotal roles in RNA metabolism, including RNA splicing, translation, and degradation. Research into Dbil5 recombinant proteins aims to elucidate the molecular mechanisms underlying these processes, particularly in the context of gene regulation and expression. Abnormalities in RNA helicase function have been implicated in various diseases, including cancer and neurodegenerative disorders, making Dbil5 a potential target for therapeutic intervention. Additionally, the recombinant protein has utility in biochemical assays, enabling the study of its enzymatic activity and interaction with RNA substrates. As researchers continue to dissect the role of Dbil5 in cellular functions, the development of recombinant Dbil5 proteins provides a valuable tool for understanding the complexities of RNA biology and the potential for innovative treatments based on helicase modulation. This ongoing research bridges gaps in our comprehension of RNA-related diseases and paves the way for advancements in molecular biology and therapeutic strategies.
