Analytical Data
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Gene name
UL128
- Application
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Alternative Names
UL128；VEGF165R2；Neuropilin-2
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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
P16837
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Expression Region
1-171aa
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AA Sequence
MSPKDLTPFLTTLWLLLGHSRVPRVRAEECCEFINVNHPPERCYDFKMCNRFTVALRCPDGEVCYSPEKTAEIRGIVTTMTHSLTRQVVHNKLTSCNYNPLYLEADGRIRCGKVNDKAQYLLGAAGSVPYRWINLEYDKITRIVGLDQYLESVKKHKRLDVCRAKMGYMLQ
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Molecular Weight
23.7 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
UL128 is a glycoprotein encoded by the human cytomegalovirus (HCMV), which is a member of the Herpesviridae family. Research on UL128 has attracted significant attention due to its critical role in viral entry and immune evasion. This protein is part of a larger complex that assists HCMV in infecting host cells, particularly endothelial and epithelial cells, which are key targets during infection. The UL128 protein has been shown to mediate the virus's interaction with specific cell surface receptors, facilitating fusion and uptake of the viral particle. Additionally, UL128 is implicated in the immune response, as it can modulate the host's immune recognition, thereby helping the virus evade detection by the immune system. Studies indicate that UL128 may also contribute to the establishment of latent infection, a hallmark of HCMV, posing challenges for vaccine development and therapeutic interventions. Consequently, understanding the structure, function, and interactions of UL128 is crucial for developing effective strategies to combat HCMV infections, which pose significant risks for immunocompromised individuals and can lead to severe complications in congenital infections. Research efforts have focused not only on the protein's role in virulence but also on its potential as a target for vaccine development, given its surface localization and involvement in the immune response. Overall, UL128 serves as a critical focal point in the ongoing endeavor to unravel the complexities of HCMV pathogenesis and to create effective preventive measures against this widespread virus.
