Analytical Data
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Gene name
D8L
- Application
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Alternative Names
D8L；Putative ATP-dependent RNA helicase DDX11-like Protein 8
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Species
E.coli
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Source
E. coli
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Tag
His tag N-Terminus
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
L7QJR5
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Expression Region
1-261aa
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AA Sequence
MPQQLSPINIETKKAISNARLKPLDIHYNESKPTTIQNTGKLVRINFKGGYISGGFLPNEYVLSSLRIYWGKEDDYGSNHLIDVYKYSGEINLVHWNKKKYSSYEEAKKHDDGLIIISIFLQVSDHKNVYFQKIVNQLDSIRSANTSAPFDSVFYLDNLLPSTLDYFTYLGTTINHSADAAWIIFPTPINIHSDQLSKFRTLLSSSNHDGKPHYITENYRNPYKLNDDTQVYYSGEIIRAATTSPARDNYFMRWLSDLRET
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Molecular Weight
37.5 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
The study of D8L recombinant protein is rooted in the quest to understand viral mechanisms and develop effective vaccines. D8L is a protein found in certain viruses, particularly within the family of Poxviridae, where it plays a crucial role in the virus's ability to evade the host immune response. By analyzing its structure and function, researchers aim to unravel the molecular interactions that D8L engages in during viral replication and immune evasion. Understanding these processes can pave the way for innovative therapeutic strategies and vaccine development, particularly in combating viral infections that have significant public health implications. Moreover, the recombinant expression of D8L in laboratory settings enables detailed studies of its properties, the characterization of its antigenicity, and its potential use as a target for vaccine creation. Such research not only enhances our fundamental understanding of virology but also contributes to broader efforts in infectious disease control and vaccine efficacy.
