Analytical Data
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Gene name
BLLF1
- Application
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Alternative Names
Membrane antigen Short name: MA
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Species
Epstein-Barr virus
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Source
E. coli
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Tag
N- His-SUMO
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
P03200
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Expression Region
1-493aa
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Molecular Weight
68.5 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
BLLF1, a protein derived from the Epstein-Barr virus (EBV), has garnered significant interest in the field of virology and immunology due to its role in modulating host immune responses. EBV, a member of the herpesvirus family, is associated with various diseases, including infectious mononucleosis and certain types of cancers, such as Burkitt lymphoma and nasopharyngeal carcinoma. The study of BLLF1 is particularly relevant as it is involved in the virus’s ability to evade the immune system, thereby facilitating persistent infections. Recent research has focused on the structural characterization of the BLLF1 protein and its interactions with host immune components, revealing its potential as a therapeutic target. Additionally, understanding the mechanisms by which BLLF1 influences immune evasion could lead to innovative approaches in the development of vaccines and treatments for EBV-associated diseases. The ongoing investigation into BLLF1’s role in viral pathogenesis underscores its significance in combating EBV-related disorders and enhancing our knowledge of herpesvirus biology.
