Analytical Data
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Gene name
BPLF1
- Application
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Alternative Names
BPLF1；Cullin-1
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Species
Human
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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
P03186
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Expression Region
1-320aa
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AA Sequence
MSNGDWGQSQRTRGTGPVRGIRTMDVNAPGGGSGGSALRILGTASCNQAHCKFGRFAGIQCVSNCVLYLVKSFLAGRPLTSRPELDEVLDEGARLDALMRQSGILKGHEMAQLTDVPSSVVLRGGGRVHIYRSAEIFGLVLFPAQIANSAVVQSLAEVLHGSYNGVAQFILYICDIYAGAIIIETDGSFYLFDPHCQKDAAPGTPAHVRVSTYAHDILQYVGAPGAQYTCVHLYFLPEAFETEDPRIFMLEHYGVYDFYEANGSGFDLVGPELVSSDGEAAGTPGADSSPPVMLPFERRIIPYNLRPLPSRSFTSDSFPA
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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
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Protein Description
BPLF1 is a multifunctional protein encoded by the Epstein-Barr virus (EBV), a member of the herpesvirus family associated with various human diseases, including infectious mononucleosis, certain malignancies, and autoimmune disorders. Research on BPLF1 has gained momentum due to its critical role in modulating the host immune response and its potential implications in virus pathogenesis. This protein possesses deubiquitinating enzyme activity, allowing it to cleave ubiquitin from host proteins, thereby evading immune detection and manipulating cellular pathways to favor viral replication. Understanding the structure and function of BPLF1 is essential for elucidating the mechanisms by which EBV persists in the host and contributes to disease. Additionally, BPLF1 may serve as a target for therapeutic intervention, making it a key focus in virology and immunology. Its study not only enhances our understanding of EBV biology but also provides insights into broader mechanisms of immune evasion by other viruses. The ongoing research into BPLF1’s interactions with host factors and its role in viral latency highlights its potential significance as a biomarker for EBV-related diseases and a candidate for developing novel antiviral strategies.
