Analytical Data
-
Gene name
UL132
- Application
-
Alternative Names
(L3)
-
Species
Human cytomegalovirus
-
Source
E. coli
-
Tag
N- MBP & C- His-Avi
-
Purity
Greater than 90% as determined by SDS-PAGE.
-
Uniprot
P69339
-
Expression Region
157-270aa
-
Molecular Weight
61.1 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
UL132 is a protein encoded by the human cytomegalovirus (HCMV), which belongs to the Herpesviridae family. Research into UL132 has gained significance due to its involvement in viral pathogenesis and immune evasion. HCMV is known for causing significant health issues, especially in immunocompromised individuals, such as organ transplant recipients and those with HIV/AIDS. Studies have suggested that UL132 plays a critical role in modulating the host immune response, allowing the virus to evade detection and persist in the host. This immunomodulatory function makes UL132 a potential target for therapeutic interventions. Understanding the molecular mechanisms by which UL132 operates can provide insights into HCMV biology and contribute to the development of antiviral strategies. Furthermore, given the increasing prevalence of viral infections and the limitations of current antiviral treatments, research into proteins like UL132 is essential for advancing our knowledge of viral-host interactions and improving patient outcomes in HCMV-related diseases.
