Analytical Data
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Gene name
UL131
- Application
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Alternative Names
UL131；Envelope glycoProtein L
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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
P16773
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Expression Region
1-76aa
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AA Sequence
MCMMSHNKAFFLSLQHAAVSGVAVCLSVRRGAGSVPAGNRGKKTIITEYRITGTRALARCPTKPVTSMWNSSWTSR
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Molecular Weight
15.2 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
UL131 is a protein associated with human cytomegalovirus (HCMV), a member of the herpesvirus family, which is a significant pathogen affecting immunocompromised individuals, including organ transplant recipients and patients with AIDS. The UL131 locus is critical for the virus's host cell entry and contributes to its ability to evade the host immune response. Recent studies have highlighted the importance of UL131 in promoting the spread of HCMV within the body, particularly its role in vascular endothelium infection, which can lead to various complications. Research has focused on understanding the mechanisms by which UL131 facilitates viral pathogenesis, including its interactions with host cell proteins and its impact on immune evasion. The elucidation of UL131's structure and function not only enhances our understanding of HCMV biology but also opens avenues for the development of targeted antiviral therapies. As vaccine development remains a challenge, characterizing UL131 could provide novel targets for therapeutic intervention, aiming to mitigate the morbidity associated with HCMV infections. Therefore, ongoing research into UL131's role in HCMV infection and pathogenesis is crucial for developing effective strategies to combat this prevalent virus.
