Protein is >95% pure as determined by 10% PAGE (coomassie staining).
The Recombinant Norovirus Group-1 Capsid, E.Coli derived, is a positive sense RNA virus with 7.5kb nucleotides, encoding a major structural protein VP1 with 50-55kDa and a VP2 protein. The full length of VP1 capsid protein is derived from the group 1 Norwalk virus. The protein is fused to a 6 His tag at N-terminal and purified by chromatography techniques.
Human norovirus is a common cause of gastroenteritis, leading to symptoms like vomiting, diarrhea, and nausea. It is classified into two groups: group 1 and group 2. Norwalk virus, discovered in 1968, belongs to group 1. The virus infects millions globally, with a high prevalence in the United States, particularly during the winter months. While most individuals recover quickly, norovirus can be severe for vulnerable populations like young children, the elderly, and those with weakened immune systems. Transmission occurs primarily through contaminated food, water, or surfaces, highlighting the importance of hygiene practices. The virus's structure, particularly the P domain within the VP1 capsid protein, is crucial for its ability to bind to human cells, making it a target for vaccine development.
This recombinant norovirus group-1 capsid protein is produced in E. coli and represents the major structural component of the virus. It is derived from the Norwalk virus strain and includes a 6-His tag for purification. The protein is supplied in a solution form and is highly pure, making it suitable for research applications.
The protein is supplied in a buffer solution containing PBS, 25mM potassium carbonate (K2CO3), and 25% glycerol.
The purity of the recombinant norovirus group-1 capsid protein is greater than 95%, as determined by SDS-PAGE analysis with Coomassie blue staining.
For short-term storage, the recombinant norovirus group-1 capsid protein can be kept at 4°C for up to 1 week. For longer-term storage, it is recommended to store the protein at or below -18°C. To maintain protein integrity and activity, avoid repeated freeze-thaw cycles.
Noroviruses are a group of viruses that cause acute gastroenteritis in humans. They are highly contagious and can spread through contaminated food, water, surfaces, and close contact with infected individuals. Norovirus infections are characterized by symptoms such as nausea, vomiting, diarrhea, and stomach cramps. These viruses are a leading cause of foodborne illness outbreaks worldwide.
Noroviruses are non-enveloped, single-stranded RNA viruses belonging to the Caliciviridae family. The viral genome is approximately 7.5 kilobases in length and is organized into three open reading frames (ORFs). The major structural protein of the virus is the capsid protein, which is encoded by ORF2. The capsid protein is responsible for forming the protective shell around the viral RNA and plays a crucial role in the virus’s ability to infect host cells.
The capsid protein of norovirus is composed of 180 copies of a single protein, VP1, which self-assembles into virus-like particles (VLPs). These VLPs are structurally and antigenically similar to the native virus but lack the viral RNA, making them non-infectious. The capsid protein is divided into two main domains: the shell (S) domain and the protruding (P) domain. The S domain forms the inner core of the capsid, while the P domain extends outward and is involved in receptor binding and immune recognition.
Recombinant norovirus capsid proteins are produced using various expression systems, including bacterial, yeast, insect, and mammalian cells. These recombinant proteins are used to study the structure and function of the virus, develop diagnostic assays, and create vaccines. The production of recombinant capsid proteins involves cloning the gene encoding the VP1 protein into an expression vector, which is then introduced into the host cells. The host cells produce the capsid protein, which can be purified and used for further research.