Analytical Data
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Gene name
BDLF3
- Application
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Alternative Names
BDLF3；
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Species
Epstein-Barr
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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
P03224
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Expression Region
29-186aa
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AA Sequence
SSTASAGNVTGTTAVTTPSPSASGPSTNQSTTLTTTSAPITTTAILSTNTTTVTFTGTTVTPVPTTSNASTINVTTKVTAQNITATEAGTGTSTGVTSNVTTRSSSTTSATTRITNATTLAPTLSSKGTSNATKTTAELPTVPDERQPSLSYGLPLWT
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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 critical protein encoded by the Epstein-Barr virus (EBV), which belongs to the herpesvirus family. This virus is known for its role in various human diseases, including infectious mononucleosis and certain malignancies, such as Hodgkin lymphoma and nasopharyngeal carcinoma. The BDLF3 protein is involved in viral replication and the modulation of host immune responses, acting as an important factor in the virus's ability to establish latency and promote persistent infection. Understanding the structure and function of BDLF3 is crucial for deciphering its role in the viral life cycle and devising potential therapeutic strategies. Recent studies have focused on characterizing the recombinant BDLF3 protein, aiming to elucidate its interactions with host cellular mechanisms, particularly in immune evasion and signaling pathways. Advances in protein expression techniques have enabled the production of BDLF3 in significant amounts, facilitating biochemical and structural analyses. Insights gained from these studies may contribute to the development of targeted antiviral therapies and vaccines, highlighting the importance of BDLF3 in the broader context of EBV-associated diseases.
