Analytical Data
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Gene name
BLLF3
- Application
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Alternative Names
/
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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
K9US42
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Expression Region
1-278aa
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Molecular Weight
46.9 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
BLLF3 (Balamp3) is a unique protein derived from the Epstein-Barr Virus (EBV), a member of the herpesvirus family, which is known for its role in various cancers and diseases, including infectious mononucleosis and lymphoproliferative disorders. Research on BLLF3 has gained significant attention due to its involvement in the viral lifecycle and its potential role in immune evasion. The protein is thought to interact with host immune responses, particularly by modulating the activity of immune cells and affecting the presentation of viral antigens. As a result, understanding the structure and function of BLLF3 is critical for developing novel therapeutic strategies, including vaccines and immunotherapies aimed at EBV-related malignancies. Structural studies and the exploration of BLLF3's biological activities are essential to uncover its mechanisms of action and its potential as a target for intervention, particularly in cancers associated with EBV. Additionally, the engineering of BLLF3 as a recombinant protein allows for further investigation into its functional roles and interactions with the immune system, thus paving the way for innovative approaches to manage diseases linked to EBV. Overall, the study of BLLF3 recombinant protein represents a promising avenue for expanding our knowledge of viral pathogenesis and enhancing therapeutic options for affected patients.
