Analytical Data
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Gene name
UL32
- Application
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Alternative Names
(150 kDa matrix phosphoprotein)(150 kDa phosphoprotein)(pp150)(Basic phosphoprotein)(BPP)(Phosphoprotein UL32)(Tegument protein UL32)
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Species
Human cytomegalovirus
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Source
E. coli
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Tag
N- MBP & C- His-Avi
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
P08318
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Expression Region
1-285aa
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Molecular Weight
81.0 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
Related Products
Protein Description
UL32, a protein encoded by the human cytomegalovirus (HCMV), plays a critical role in the virus's lifecycle and pathogenesis. This protein is part of the UL128L complex, which is essential for the virus's ability to enter host cells and establish infection. Research into UL32 has gained momentum due to its implications in HCMV-related diseases, particularly in immunocompromised individuals, such as organ transplant recipients and HIV-infected patients, where HCMV can lead to severe complications. Understanding the structure and function of UL32 can provide insights into the mechanisms of viral entry, immune evasion, and the development of potential therapeutic interventions. Additionally, UL32's interaction with other viral and host proteins makes it a target of interest for vaccine and antiviral drug development. Recent studies have also indicated that UL32 may influence the immune response, raising questions about its role in viral latency and reactivation. Thus, the study of UL32 not only enhances our understanding of HCMV biology but also holds promise for the development of novel strategies to combat HCMV-associated diseases. The growing interest in this protein underscores its significance as a potential biomarker for disease severity and as a focal point for therapeutic targeting in the quest to mitigate HCMV's impact on public health.
