Analytical Data
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Gene name
UL111A
- Application
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Alternative Names
UL111A；IL10R；Interleukin-10 receptor subunit alpha
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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
F5HC71
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Expression Region
26-176aa
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AA Sequence
ATTTTIKNTKPQCRPEDYATRLQDLRVTFHRVKPTLQREDDYSVWLDGTVVKGCWGCSVMDWLLRRYLEIVFPAGDHVYPGLKTELHSMRSTLESIYKDMRQCPLLGCGDKSVISRLSQEAERKSDNGTRKGLSELDTLFSRLEEYLHSRK
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Molecular Weight
36.0 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
UL111A, a protein encoded by the human cytomegalovirus (HCMV), plays a crucial role in the virus's ability to evade the host immune response. Identified as a multifunctional protein, UL111A functions primarily as a glycoprotein that interacts with various immune receptors, leading to the modulation of immune signaling pathways. Research has shown that UL111A can inhibit the activation of natural killer (NK) cells and T cells, thereby promoting viral persistence and latency. Studies indicate that UL111A achieves this by mimicking host proteins and interfering with cytokine signaling, which are critical for immune activation. Given the prevalence of HCMV in the human population and its potential to cause severe disease in immunocompromised individuals, along with its association with various conditions, including congenital infections and organ transplant rejection, understanding UL111A's mechanisms is essential for developing therapeutic interventions. Recent advancements in recombinant protein technology have enabled the production of UL111A for detailed structural and functional analysis, paving the way for novel vaccine strategies and antiviral therapies that target this viral evasion mechanism. The study of UL111A is not only significant for HCMV pathology but also offers broader insights into viral-host interactions, making it a key target in virology research.
