Analytical Data
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Gene name
VB6
- Application
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Alternative Names
VB6；Negative regulator YfiR
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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
Q9I4L4
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Expression Region
1-190aa
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AA Sequence
MPSLPTLQPLDLYRRTLACLVLAVSCLGGGGLWADDARTSIEQRSNAVSQVLLGIFSYVRWPKEPAVLQLCVVGPTEYADGLLRGMVQANGRRVHAERRAVDNPDLGTLCNVIYLGVVDERERQQVFRSLAGHPVLSISERGTECSVGSMFCLNVGGPRITFEANLDSIARSGVRVHPSVLKLARRQATP
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Molecular Weight
20.6 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
VB6, a variant of the well-studied HBV (Hepatitis B Virus) core protein, has garnered attention in the field of molecular biology and virology due to its potential role in vaccine development and therapeutic applications. Research into recombinant VB6 proteins is driven by the urgent need for effective vaccines against HBV, which poses significant health risks globally, affecting millions of individuals. The ability to produce VB6 as a recombinant protein allows for detailed studies into its structure and function, facilitating the understanding of its immunogenic properties. This protein can be engineered to present HBV antigens in a way that elicits a robust immune response, which is crucial for vaccine efficacy. Furthermore, exploring VB6's interactions with host immune cells provides insights into viral pathogenesis and potential immune evasion mechanisms. Recent advancements in recombinant DNA technology have made it feasible to generate large quantities of VB6 proteins, enabling comprehensive biochemical and biophysical characterization. The ongoing research aims to optimize these recombinant proteins to enhance their immunogenicity and applicability in clinical settings, thereby contributing to the fight against HBV and improving public health outcomes.
