Analytical Data
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Gene name
BPLF1
- Application
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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
P03186
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Expression Region
1-320aa
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Molecular Weight
41.9 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
BPLF1, a viral protein derived from the Epstein-Barr virus (EBV), has garnered significant attention in the field of virology and immunology due to its unique role in modulating host immune responses. EBV, a member of the Herpesviridae family, is associated with various pathologies, including infectious mononucleosis and certain malignancies such as Hodgkin's lymphoma and nasopharyngeal carcinoma. The BPLF1 protein functions primarily as an E3 ubiquitin ligase, facilitating the degradation of host proteins that are critical for antiviral immunity. This capability allows EBV to evade host immune surveillance, making BPLF1 a crucial factor in the persistence and pathogenicity of the virus. Research on BPLF1 encompasses its structural characterization, enzymatic function, and interactions with host cellular machinery, with the aim of understanding its mechanisms of immune evasion. Furthermore, studies have indicated that BPLF1 may play a role in promoting viral replication and latency, emphasizing its potential as a therapeutic target. Investigating BPLF1 not only provides insights into EBV biology but also contributes to broader knowledge regarding virus-host interactions and immune regulation, thus holding promise for the development of novel antiviral strategies.
