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UL2

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All listed services and products are For Research Use Only. Do Not use in any diagnostic or therapeutic applications.

Background

UL2 protein is an early localized uracil -DNA glycosidase (UDG) encoded by herpes simplex virus HSV-1 and related α herpes virus UL2. It starts expression at the very early transcription stage of the virus, can be transported to the host cell nucleus and enriched in the viral DNA replication region, and participates in the whole process of viral genome replication. There is a significant functional difference between UL2, a virus source, and the endogenous NG repair enzyme in human body. UL2 has a unique dual biological activity, which can not only specifically remove the uracil residues mistakenly mixed into the virus genome in the process of latent infection and cleavage and replication, but also directly bind the p65/p50 NF-κB subunit, specifically inhibit the host's pro-inflammatory immune signal cascade reaction and mediate virus immune escape. Under the latent infection state of sensory neurons, low-level continuous expression of UL2 can resist the deamination damage of cytosine, maintain the structural integrity of free virus DNA and ensure the latent steady state of the virus; In the activation stage of virus lysis, the up-regulation of UL2 expression can support the high-fidelity amplification of virus genome, and at the same time passivate the antiviral defense response mediated by host cytokines, which helps the virus to proliferate efficiently. Host cell glycosidase can't compensate for the unique dual functions of virus DNA repair and immunosuppression of UL2, and knocking out UL2 will significantly weaken the replication ability and reactivation efficiency of herpes virus, which is an irreplaceable core target for the study of herpes virus DNA repair mechanism and the screening of anti-herpes virus drugs.

UL2 locates in the viral DNA replication complex in the nucleus, and simultaneously exerts the dual effects of viral genome repair and host immunosuppression. It relies on the conserved UDG catalytic domain to identify uracil mismatch DNA sites and initiate damage excision and repair, and at the same time dissociates NF-κB dimer through independent domain, blocking the transcription activation of downstream target genes. The unique bifunctional structural model of this virus clearly differentiated from the host monofunctional uracil glycosidase, making UL2 a key viral effector protein integrating genome homeostasis maintenance and immune escape regulation. UL2-mediated DNA repair and NF-κB inhibition pathway can accurately link virus replication cycle and host inflammatory immune response, and dynamically balance the process of virus latent survival and cleavage and amplification according to infection stage. UL2 is mainly involved in the maintenance of latent steady state of virus in neurons and the proliferation and spread of virus in epithelial cells. The loss of UL2 function will lead to the accumulation of uracil damage in viral genome, and at the same time, it will relieve the host's antiviral inflammation inhibition and restart the antiviral immune response of powerful organism. To sum up, UL2 is the key target for the analysis of enzymatic mechanism of herpes virus and the research and development of antiviral targeted therapy.

Fig. 1 Schematic of full-length HSV-1 UL2 and truncated mutants, marking N-terminal nuclear localization signals (NLS) and nuclear export signal (NES). (OA Literature)Fig. 1 Linear structural diagram of HSV-1 UL2. Full-length UL2 contains two N-terminal nuclear localization sequences and one nuclear export motif; truncated variants were constructed to verify subcellular localization functional domains.1

UL2 Protein Function: Core Roles in Viral UDG Repair and Host NF-κB Inhibition

The biological functions of UL2 are fully focused on viral uracil excision and inflammatory pathway suppression:

  • Viral UDG Catalysis: Removes misincorporated uracil from replicating herpes viral DNA strands.
  • NF-κB Signal Blocking: Sequesters p65/p50 subunits to suppress host pro-inflammatory transcription.
  • Latency Genome Preservation: Maintains intact episomal viral DNA in resting sensory neurons.
  • Lytic Replication Support: Boosts high-fidelity viral genome amplification during reactivation.
  • Disease Relevance: UL2 deletion attenuates HSV replication and viral neurovirulence phenotypes.

UL2 Protein Product

Creative Biolabs offers high-quality UL2 proteins through optimized eukaryotic/viral expression systems, including full-length nuclear viral protein and isolated UDG catalytic domain variants. These products retain native uracil excision and NF-κB binding dual activity, suitable for viral DNA repair and anti-herpes inhibitor screening assays. All UL2 proteins undergo strict quality control to ensure consistent performance and reliable application across virology research platforms.

UL2 Protein Product

Not finding the protein product you need? Contact us to start your one-stop custom service!

UL2 Stable Cell Line Product

Creative Biolabs provides custom-engineered UL2 stable cell lines, including viral mimic overexpression and blank empty vector control models. These cell lines are optimized for viral enzyme profiling and host immune signal functional analysis. Each cell line undergoes stringent validation to ensure stable expression profiles during long-term neuronal cell culture, and can be widely deployed for anti-herpes small molecule screening workflows.

UL2 Stable Cell Line Product

Not finding the stable cell line product you need? Contact us to start your one-stop custom service!

UL2 Recombinant Antibody Product

High-specificity recombinant antibodies targeting UL2 are developed via advanced antibody engineering technologies, with no cross-reactivity with human endogenous UNG glycosylase. These antibodies are validated for infected cell nuclear localization detection and neuronal tissue viral expression profiling, and can be combined with viral DNA polymerase marker reagents to analyze viral replication complexes in host cell models.

UL2 Recombinant Antibody Product

Not finding the recombinant antibody product you need? Contact us to start your one-stop custom service!

Product Features

  • Native UDG & NF-κB Binding Dual Activity: Preserves intact viral genome repair and immune evasion capacity for herpes virology research.
  • UL2 Viral Specificity: Eliminates non-specific cross-recognition of human cellular UNG enzymes.
  • Antiviral Compatibility: Optimized reagent series for HSV replication inhibitor screening workflows.
  • Comprehensive Customization Support: Facilitates end-to-end development of customized proteins, antibodies and stable cell lines to address viral DNA repair research demands.

Custom UL2 Research Services

Beyond catalog products, Creative Biolabs offers specialized custom services for UL2 research:

  • Custom UL2 Protein Production: Tailored expression of mutant and tagged UL2 constructs for UDG/NF-κB binding analysis.
  • Custom Antibody Development: Generation of UL2-specific antibodies for virus-infected nuclear immunostaining.
  • Stable Cell Line Engineering: Construction of UL2-expressing neuronal host cell models.
  • Functional Assay Development: Custom design of viral DNA uracil repair detection workflows.

Frequently Asked Questions (FAQ)

  1. What is the primary function of UL2?

    UL2 is herpes viral uracil-DNA glycosylase that repairs viral DNA and inhibits host NF-κB antiviral inflammation.

  2. Why is UL2 a significant research target?

    UL2 is required for efficient HSV latency maintenance and lytic viral reactivation in sensory neurons.

  3. Are Creative Biolabs' UL2 products suitable for clinical use?

    No, all UL2 products and services are strictly for research use only, not intended for clinical antiviral therapy.

  4. What types of UL2 products does Creative Biolabs offer?

    Offerings include full-length viral UL2 enzymes, virus-specific detection antibodies and custom stable cell lines for herpes research.

  5. How are UL2 proteins validated for activity?

    UL2 proteins are validated via uracil DNA excision and NF-κB co-binding functional testing.

Reference
  1. Li, Meili, et al. "The nuclear localization signal-mediated nuclear targeting of herpes simplex virus 1 early protein UL2 is important for efficient viral production." Aging (Albany NY) 12.3 (2020): 2921. Under Open Access license CC BY 3.0, without modification. https://doi.org/10.18632/aging.102786
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