Analytical Data
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Gene name
D13L
- Application
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Alternative Names
(62 kDa protein)(Rifampicin resistance protein)
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Species
Vaccinia virus
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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
P68441
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Expression Region
1-230aa
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Molecular Weight
33.2 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 D13L protein, a member of the vaccinia virus genome, has garnered significant interest in virology research due to its potential roles in immune evasion and pathogenesis. This protein is a part of the large family of viral proteins that modulate host immune responses, particularly by interfering with cytokine signaling pathways. Studies have shown that D13L can inhibit the action of type I interferons, which are crucial for the antiviral response, thereby allowing the virus to replicate more effectively within the host. Furthermore, the structure of D13L suggests that it may have unique binding capabilities that facilitate its interaction with host cell components. Understanding the precise mechanisms by which D13L functions not only provides insights into viral strategies for immune evasion but also opens avenues for developing novel therapeutic approaches against viral infections. This research is particularly relevant in the context of emerging viruses and the need for effective antiviral therapies, making D13L a target of interest in the ongoing efforts to mitigate the impact of viral diseases on public health.
