Analytical Data
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Gene name
nsP4
- Application
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Alternative Names
Polyprotein nsP1234
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Species
Chikungunya virus
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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
Q8JUX6
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Expression Region
2228-2474aa
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Molecular Weight
31.1 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
The nsP4 protein, a critical component of the replication complex of alphaviruses, plays a significant role in RNA synthesis and viral pathogenesis. Research into nsP4 is vital due to its dual function in both genome replication and sub-genomic RNA synthesis, thus influencing viral infection cycles. Its exceptional RNA-dependent RNA polymerase activity enables the synthesis of viral RNA, making it a prime target for antiviral drug development. Furthermore, understanding the structural and functional characteristics of nsP4 can provide insights into the mechanisms of viral replication and host interaction, which are essential for developing effective therapeutic strategies against alphavirus infections. Given the rising incidence of alphavirus-related diseases globally, including chikungunya and Ross River virus, studies on nsP4 are becoming increasingly important for public health. Recent advances in techniques such as cryo-electron microscopy and X-ray crystallography have facilitated the detailed study of nsP4's structure, revealing potential sites for inhibitors. Overall, focused research on nsP4 not only contributes to our basic understanding of viral replication mechanisms but also aids in the pursuit of novel antiviral therapies, highlighting its significance in virology.
