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Recombinant Norwalk Virus Capsid Protein, N-His

Cat. No.VG9C363

Product TypeVeterinary Antigens

Size

Product Overview

BioVenic's Recombinant Norwalk Virus Capsid Protein, N-His is a recombinant protein expressed from E.coli. Its predicted molecular weight is 36.8 kDa. The purity is>90% (SDS-PAGE).

Specifications

Type Recombinant Protein
Species Virus
Expression System E.coli
Purity >90% (SDS-PAGE)
Predicted Molecular Weight 36.8 kDa
Physical State Lyophilized
Formulation The buffer before lyophilization is a solution in PBS pH 7.4, 0.02% NLS, 1mM EDTA, 4% Trehalose, 1% Mannitol.

Target Information

In veterinary medicine, the Norwalk Virus Capsid Protein plays a crucial role in virus assembly, infection mechanisms, and vaccine development. As the main structural protein of norovirus, it is responsible for forming the virus shell and can self-assemble into virus-like particles (VLPs), which are similar in size and appearance to native virus particles. These VLPs have significant antigenicity and can induce norovirus-specific serum antibodies in laboratory animals. Moreover, the Capsid Protein is key in virus-host cell receptor recognition, invasion, and immune response, making it a primary target for vaccines and therapeutic strategies.

Protein Norwalk Virus Capsid Protein
Protein Synonym Capsid Protein
UniProt ID Q5F4T5

Shipping and Storage

This product is shipped with dry ice. Avoid repeated freezing and thawing. Store at -20°C/-80°C upon receipt, aliquoting is necessary for mutiple use.

Documents

COA

To request a Certificate of Analysis, please enter the Lot No. in the search box. Note: Certificate of Analysis not available for kits.

The product is for research use only.
Not for commercial, prophylactic, diagnostic, or therapeutic applications.

User Note

  1. Always centrifuge tubes before opening. Avoid mixing by vortexing or pipetting. Reconstitute to a concentration more than 100 μg/ml is recommended. Dissolve the lyophilized protein in distilled water.Aliquote the reconstituted solution to minimise freeze-thaw cycles.
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