Analytical Data
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Gene name
UL130
- Application
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Alternative Names
UL130Uncharacterized protein UL130
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Species
Human cytomegalovirus
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Source
E. coli
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Tag
N- His-SUMO
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
P16772
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Expression Region
26-214aa
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Molecular Weight
37.7 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
Related Products
Protein Description
UL130 is a protein encoded by the human cytomegalovirus (HCMV), a member of the Herpesviridae family, which plays a critical role in the virus's life cycle and pathogenesis. Research on UL130 is particularly significant due to the clinical implications of HCMV, which can cause severe diseases in immunocompromised individuals, such as organ transplant recipients and those with HIV/AIDS. UL130 is known to be involved in viral entry and immune evasion, making it a potential target for therapeutic interventions. Studies have demonstrated that UL130 can modulate host immune responses, facilitating viral persistence and latency. Recent investigations have focused on the structure-function relationships of UL130, examining how its molecular characteristics influence HCMV infectivity and the immune response. Understanding the role of UL130 at a molecular level could pave the way for the development of novel antiviral strategies, improving outcomes for at-risk populations. Furthermore, insights gained from UL130 studies promise to contribute to the broader understanding of herpesvirus biology and host-pathogen interactions. Overall, ongoing research into UL130 and its functionalities not only reveals the intricacies of HCMV pathogenesis but also holds promise for enhancing therapeutic options against this prevalent virus.
