Analytical Data
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Gene name
BLLF3
- Application
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Alternative Names
BLLF3；Deoxyuridine 5'-triphosphate nucleotidohydrolase
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Species
E.coli
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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
K9US42
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Expression Region
1-278aa
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AA Sequence
MEACPHIRYAFQNDKLLLQQASVGRLTLVNKTTILLRPMKTTTVDLGLYARPPEGHGLMLWGSTSRPVTSHVGIIDPGYTGELRLILQNQRRYNSTLRPSELKIHLAAFRYATPQMEEDKGPINHPQYPGDVGLDVSLPKDLALFPHQTVSVTLTVPPPSIPHHRPTIFGRSGLAMQGILVKPCRWRRGGVDVSLTNFSDQTVFLNKYRRFCQLVYLHKHHLTSFYSPHSDAGVLGPRSLFRWASCAFEEVPSLAMGDSGLSEALEGRQGRGFGSSGQ
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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
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Protein Description
BLLF3, an Epstein-Barr virus (EBV) encoded protein, plays a crucial role in the virus's life cycle and its ability to evade the host's immune response. Research into BLLF3 is primarily focused on its function as an immunoevasin, which helps EBV to persist in human cells by modulating the host's immune recognition mechanisms. BLLF3 interacts with major histocompatibility complex (MHC) class I molecules, preventing their expression on the surface of infected cells and thus facilitating viral latency. This characteristic is particularly significant as EBV is associated with various malignancies, including Hodgkin's lymphoma and nasopharyngeal carcinoma. Understanding the structure and function of BLLF3 can provide valuable insights into the mechanisms of viral persistence and immune evasion, opening avenues for potential therapeutic interventions. Additionally, the development of BLLF3 as a target for vaccine design or immunotherapy could enhance strategies aimed at controlling EBV-related diseases. As research progresses, elucidating the molecular details of BLLF3's interactions and its impact on immune modulation will be critical in formulating effective treatment strategies for EBV-associated conditions.
