Analytical Data
-
Gene name
BRLF1
- Application
-
Alternative Names
Immediate-early protein Rta
-
Species
Epstein-Barr virus
-
Source
E. coli
-
Tag
N- His & C- Myc
-
Purity
Greater than 90% as determined by SDS-PAGE.
-
Uniprot
Q3KSS7
-
Expression Region
352-605aa
-
Molecular Weight
34.9 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
BRLF1 is a transcriptional regulator crucial for the reactivation of Epstein-Barr Virus (EBV) from latency, playing a significant role in the virus's lifecycle and its associated diseases, including various lymphoproliferative disorders. As a member of the RING finger protein family, BRLF1 not only influences viral gene expression but also interacts with host cellular factors, potentially leading to oncogenic transformations. The study of BRLF1 recombinant protein is vital for understanding its functional mechanisms in viral reactivation and pathogenesis. Researchers are particularly interested in elucidating its structural features, interactions with other viral and host proteins, and its role in modulating host immune responses. Characterizing BRLF1 in a recombinant form allows for detailed biochemical analyses and therapeutic explorations, including the development of vaccines or antiviral drugs targeting EBV. Furthermore, understanding BRLF1's function could provide insights into the broader implications of viral latency and reactivation, enhancing our comprehension of viral replication dynamics and their impacts on human health. Thus, BRLF1 recombinant protein research holds promise for advancing both virology and clinical applications related to EBV infections.
