Analytical Data
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Gene name
BDLF3
- Application
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Alternative Names
BDLF3Glycoprotein BDLF3
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Species
Epstein-Barr virus
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Source
E. coli
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Tag
N- His & C- Myc
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
P03224
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Expression Region
29-186aa
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Molecular Weight
22.7 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
BDLF3 is a recombinant protein derived from the Epstein-Barr virus (EBV), a common human herpes virus known for its role in infectious mononucleosis and its association with various cancers. Research into BDLF3 has gained attention due to its potential implications in understanding EBV pathogenesis and immune evasion mechanisms. BDLF3 is hypothesized to play a crucial role in the virus's life cycle, particularly in modulating the host's immune response. Studies have indicated that this protein may interfere with antigen presentation and T-cell activity, thus aiding in viral persistence. The exploration of BDLF3 as a target for therapeutic interventions is particularly significant given the global prevalence of EBV and its link to malignancies such as Burkitt lymphoma and nasopharyngeal carcinoma. By investigating the structural and functional characteristics of BDLF3, researchers aim to develop strategies that could enhance the efficacy of vaccines or immunotherapies against EBV-related diseases. Furthermore, understanding how BDLF3 interacts with host cellular mechanisms can provide insight into broader viral-host interactions, contributing to the development of novel antiviral therapies. Consequently, BDLF3 represents a focal point in the ongoing research aimed at unraveling the complexities of EBV biology and its impact on human health.
