Analytical Data
-
Gene name
BALF5
- Application
-
Alternative Names
BALF5DNA polymerase catalytic subunit; EC 2.7.7.7
-
Species
Epstein-Barr virus
-
Source
E. coli
-
Tag
N- His-SUMO
-
Purity
Greater than 90% as determined by SDS-PAGE.
-
Uniprot
P03198
-
Expression Region
1-210aa
-
Molecular Weight
39.2 kDa
-
Endotoxin
< 1.0 EU per μg protein as determined by the LAL method.
-
Form
Freeze-dried powder
-
Buffer formulation
PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300.
-
Reconstitution
Reconstitute in ddH2O to a concentration of 0.1-0.5 mg/mL. Do not vortex.
- Customization
-
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.
-
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.
-
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
BALF5, a protein encoded by the Epstein-Barr Virus (EBV), plays a critical role in viral replication and pathogenesis. As a member of the viral protein family, BALF5 is recognized for its involvement in the regulation of viral DNA synthesis, exhibiting characteristics akin to DNA polymerases. Research has highlighted BALF5’s essential function in the viral life cycle, where it contributes to the maintenance of viral genomes within host cells. Given that EBV is linked to several human malignancies, such as lymphomas and nasopharyngeal carcinoma, understanding BALF5’s structure and function can provide valuable insights into viral biology and pathology. Studies have focused on characterizing BALF5’s interactions with host cellular machinery, as well as its potential as a target for antiviral therapies. Furthermore, recombinant BALF5 protein has been produced for functional assays and structural analysis, facilitating the development of specific inhibitors that could impede viral replication. Overall, unraveling the intricate mechanisms of BALF5 not only enhances our comprehension of EBV biology but also paves the way for novel therapeutic strategies against EBV-associated diseases.
