Vaccine Lab / Alfa Chemistry
Norovirus GI.3 VP1 Virus-Like Particles

Norovirus GI.3 VP1 Virus-Like Particles

Product Name: Norovirus GI.3 VP1 Virus-Like Particles
Catalog Number: ACVL-VLP007
Category: Virus-Like Particles (VLPs)
Expression System: HEK293 (Mammalian)
Purity: >50% (SDS-PAGE)

Product Overview

Alfa Chemistry offers high-quality recombinant Norovirus GI.3 Virus-Like Particles (VLPs) derived from the Hu/GI.3/JKPG_881/SWE/2007 strain. Produced using a mammalian HEK293 expression system, these VLPs exhibit native-like structural characteristics and biologically relevant protein conformation.

The particles are generated through transient expression of the major capsid protein VP1, which spontaneously self-assembles into an icosahedral architecture. As these VLPs lack viral genomic RNA and non-structural proteins, they are non-infectious and replication-deficient, providing a safe and reliable surrogate for virology research, diagnostic development, and vaccine studies.

Key Features & Advantages

  • Mammalian Expression System: Produced in HEK293 cells to support native-like protein folding and post-translational characteristics.
  • Native-Like Capsid Structure: Composed of approximately 180 VP1 monomers forming an icosahedral particle that closely mimics the morphology of native virions.
  • Preserved Functional Domains: Maintains the S (Shell) domain for capsid assembly and the P (Protruding) domain (P1/P2) for receptor interaction and antigenic studies.
  • High Biosafety Profile: Genome-free and replication-deficient, enabling safe handling in standard laboratory environments.
  • Application-Optimized: Suitable for serological assay development, antibody screening, and epitope mapping.

Background & Scientific Significance

Noroviruses are a leading cause of global outbreaks of acute viral gastroenteritis. Within Genogroup I, the GI.3 genotype represents an important target for epidemiological studies and multivalent vaccine development.

The VP1 capsid protein plays a central role in viral assembly and immune recognition. The P2 subdomain, located within the protruding domain, is highly variable and serves as a key site for interaction with host histo-blood group antigens (HBGAs) as well as neutralizing antibodies. Utilizing GI.3 VLPs enables precise investigation of:

  • Neutralization Profiles: Evaluation of monoclonal antibodies targeting GI.3-specific epitopes
  • Assay Development: Establishment of ELISA and rapid diagnostic platforms
  • Capsid Structure & Stability: Analysis of VP1 dimerization and capsid dynamics

Related Norovirus VLP Products

In addition to Norovirus GI.3 VP1 Virus-Like Particles, Alfa Chemistry also offers a comprehensive portfolio of Norovirus VLPs covering multiple clinically relevant genotypes, including:

  • Norovirus GII.2 VLP
  • Norovirus GII.3 VLP (Hu/GII.3/SW4/2012/TN)
  • Norovirus GII.4 VLP
  • Norovirus GII.6 VLP
  • Norovirus GII.10 VLP
  • Norovirus GII.17 VLP
  • Norovirus GIX.1 VLP

These products support comparative studies, multivalent vaccine development, and broad-spectrum immunological research across different Norovirus genotypes.

For detailed specifications or custom requirements, please feel free to contact us.

Our products and services are for research use only and cannot be used for any clinical purposes.

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