HCV NS3, HRP
Description
Product Specs
Product Science Overview
Hepatitis C Virus (HCV) is a member of the Flaviviridae family, harboring an approximately 9.6 kbp positive single-stranded RNA genome . Upon infection of hepatocytes, the genome is released in the cytoplasm where the single open reading frame (ORF) is transcribed into a polyprotein using an internal ribosome entry site (IRES) sequence . Viral and cellular proteases are responsible for the cleavage and production of 10 viral proteins: structural proteins Core, E1, and E2, and non-structural proteins P7, NS2, NS3, NS4A, NS4B, NS5A, and NS5B .
Nonstructural protein 3 (NS3), also known as p-70, is a viral nonstructural protein that is a 70 kDa cleavage product of the hepatitis C virus polyprotein . It acts as a serine protease, and the C-terminal two-thirds of the protein also acts as a helicase and nucleoside triphosphatase . The first (N-terminal) 180 amino acids of NS3 have an additional role as cofactor domains for the NS2 protein .
NS3 is a bifunctional enzyme with serine protease and helicase activity . The serine-type protease region of NS3 is responsible for most of the cleavages of the viral polyprotein that free nonstructural proteins . Research indicates that NS3 is implicated in several carcinogenic processes such as proliferative signaling, cell death resistance, genomic instability and mutations, invasion and metastasis, tumor-related inflammation, immune evasion, and replicative immortality . Understanding the direct impact of viral proteins such as NS3 on cellular transformation is crucial for elucidating HCV’s role in hepatocellular carcinoma (HCC) development .
Horseradish peroxidase (HRP) is an enzyme that has been the subject of scientific research for centuries . It has been used extensively as a reporter enzyme in diagnostics and histochemistry and still plays a major role in these applications . Numerous studies have been conducted on the role of horseradish peroxidase in the plant and its catalytic mechanism . However, little progress has been made in its recombinant production .
Commercial preparations of horseradish peroxidase are still isolated from plant roots . These preparations are commonly mixtures of various isoenzymes of which only a small fraction has been described so far . The composition of isoenzymes in these mixed isolates is subjected to uncontrollable environmental conditions .
Recent advancements have led to the development of scalable recombinant HRP production processes in Escherichia coli that yield a highly pure, active, and homogeneous single isoenzyme . This recombinant HRP is comparable in its spectral and catalytic characteristics to the native plant peroxidase . The recombinant production of HRP is particularly interesting for therapeutic applications due to its high purity and consistency .
