Analytical Data
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Gene name
HCV-NS5a
- Application
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Alternative Names
BTBD1;C15orf1;NS5ATP8;BTB/POZ domain-containing Protein 1
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Species
Human
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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
Q15004
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Expression Region
1-111aa
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AA Sequence
MVRTKADSVPGTYRKVVAARAPRKVLGSSTSATNSTSVSSRKAENKYAGGNPVCVRPTPKWQKGIGEFFRLSPKDSEKENQIPEEAGSSGLGKAKRKACPLQPDHTNDEKE
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Molecular Weight
39.0kDa
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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
HCV (Hepatitis C virus) NS5A is a crucial component of the viral replication machinery and has emerged as an important target for antiviral therapy. As a multifunctional protein, NS5A plays a significant role in viral RNA replication, assembly, and immune evasion. Its involvement in these processes makes understanding its structure and function essential for developing effective treatments against HCV infection. The emergence of direct-acting antiviral agents (DAAs) that target NS5A has significantly transformed the landscape of HCV therapy, leading to high rates of sustained virologic response in infected patients. However, the presence of resistant variants and the complexity of NS5A's interactions with host cell factors underline the need for further research. The recombinant production of HCV NS5A proteins allows for the detailed study of their biochemical properties, interactions, and the mechanisms of resistance. This research contributes to elucidating the viral lifecycle and aids in the rational design of novel therapeutic strategies, ultimately improving treatment outcomes for patients suffering from chronic hepatitis C.
