Purified by proprietary chromatographic technique.
Hepatitis C Virus (HCV) is a significant global health concern, affecting millions of people worldwide. The virus is known for causing chronic liver diseases, including cirrhosis and hepatocellular carcinoma. The HCV genome encodes a single polyprotein that is processed into structural and non-structural proteins. Among these, the non-structural protein 4 (NS4) plays a crucial role in the virus’s life cycle and pathogenesis.
The NS4 protein of HCV is divided into two regions: NS4A and NS4B. NS4A acts as a cofactor for the NS3 serine protease, which is essential for the cleavage of the non-structural region of the polyprotein . NS4B, on the other hand, is involved in the formation of the membranous web, a structure critical for HCV RNA replication . Together, these proteins contribute to the virus’s ability to replicate and evade the host immune response.
Recombinant NS4 proteins are produced using various expression systems, with Escherichia coli being one of the most common . These recombinant proteins are often used in research to study the virus’s biology and to develop diagnostic assays and potential therapeutic interventions. The recombinant NS4 protein is typically expressed with a high degree of purity, often exceeding 95% .
Rhodamine is a fluorescent dye commonly used in biological research. When conjugated to proteins, it allows for the visualization and tracking of these proteins in various experimental setups. Rhodamine-labeled recombinant NS4 proteins are particularly useful in studying the interactions and localization of the NS4 protein within host cells .