Analytical Data
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Gene name
K3L
- Application
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Alternative Names
K3L; Protein K3
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Species
Vaccinia virus
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Source
E. coli
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Tag
N- His-SUMO
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
P20639
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Expression Region
1-88aa
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Molecular Weight
26.5 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 K3L protein, derived from the vaccinia virus, has garnered significant attention in molecular biology and virology due to its unique ability to inhibit host cell antiviral responses. Research into K3L has primarily focused on its role as a sense RNA-binding protein that prevents the phosphorylation of eIF2α (eukaryotic translation initiation factor 2 alpha), thereby allowing viral mRNA to be translated in the presence of interferon-induced stress. This characteristic makes K3L a potential candidate for studying viral mechanisms of immune evasion and has implications for developing novel antiviral therapies. The investigation of K3L also provides insights into the intricate interactions between viruses and host cells, contributing to our understanding of pathogenesis and immune response modulation. Furthermore, the study of K3L's structural and functional properties aids in the exploration of targeted strategies in vaccine design and therapeutic interventions against viral infections. Researchers are continually unraveling the nuances of K3L's interactions at the molecular level, revealing its potential as a model for understanding viral resistance and the broader implications for infectious disease control.
