Analytical Data
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Gene name
BHRF1
- Application
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Alternative Names
Early antigen protein R
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Species
Epstein-Barr 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
P03182
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Expression Region
1-142aa
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Molecular Weight
19.8 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
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Protein Description
BHRF1 is a protein encoded by the Epstein-Barr virus (EBV), which is a member of the herpesvirus family and is associated with various lymphoproliferative disorders and malignancies. Research surrounding BHRF1 has garnered significant attention due to its role in modulating host immune responses and promoting virus persistence. BHRF1 shares structural similarities with the cellular Bcl-2 family of proteins, which are known to regulate apoptosis and enhance cell survival. As a viral homolog, BHRF1 contributes to EBV's ability to evade the host’s immune system by inhibiting apoptosis of infected B cells, thereby facilitating prolonged infection and potential oncogenesis. Understanding the functional mechanisms of BHRF1, particularly in terms of its interaction with host cell pathways, is essential for developing therapeutic strategies to combat EBV-associated diseases. Recent advances in recombinant protein technology have facilitated the production and study of BHRF1, allowing researchers to elucidate its structure-function relationships and investigate its potential as a target for antiviral therapies. Moreover, the exploration of BHRF1's role in immune evasion and cell survival not only enhances our understanding of EBV biology but also provides insights into the broader implications of viral proteins in cancer development. As such, BHRF1 is a compelling subject for further investigation, with the potential to inform both basic virology and clinical approaches to EBV-related pathologies.











