HCV NS5, HRP
Description
Product Specs
Product Science Overview
Hepatitis C virus nonstructural protein 5A (NS5A) is a zinc-binding and proline-rich hydrophilic phosphoprotein that plays a crucial role in the replication of Hepatitis C virus RNA . NS5A is derived from a large polyprotein that is translated from the Hepatitis C virus genome and undergoes post-translation processing by nonstructural protein 3 (NS3) viral protease . Despite lacking inherent enzymatic activity, NS5A’s function is mediated through interaction with other nonstructural viral and cellular proteins .
NS5A has two phosphorylated forms: p56 and p58, which differ in electrophoretic mobility . The p56 form is basally phosphorylated by host cellular protein kinase, while p58 is a hyper-phosphorylated form . The N-terminal 30 amino acids of NS5A form an amphipathic α-helix essential for modulating the association between NS5A and the endoplasmic reticulum membrane . NS5A has three structurally different domains, with domain I being an alternative dimeric structure, while domains II and III remain unfolded .
NS5A is a critical component during Hepatitis C virus replication and subcellular localization . It modulates the polymerase activity of NS5B, an RNA-dependent RNA polymerase . Additionally, NS5A is a key mediator in regulating host cell function and activity upon Hepatitis C virus infection . Due to its essential role in viral replication, assembly, and egress, NS5A is considered a potential drug target for antiviral therapeutic intervention .
Horseradish peroxidase is an enzyme that has been extensively studied for centuries and is widely used as a reporter enzyme in diagnostics and histochemistry . It catalyzes various oxidative reactions in which electrons are transferred to peroxide species, often hydrogen peroxide, and substrate molecules are oxidized . Despite its long history of use, commercial preparations of horseradish peroxidase are still isolated from plant roots, which are mixtures of various isoenzymes .
Recombinant production of horseradish peroxidase has gained interest due to its broad applicability in medicine, life sciences, and biotechnology . Recent advancements have focused on developing scalable recombinant production processes in Escherichia coli, yielding highly pure, active, and homogeneous single isoenzymes . These recombinant enzymes are particularly interesting for therapeutic applications due to their consistent quality and high yield .
Recombinant horseradish peroxidase has shown potential in various fields, including cancer therapy, biosensor systems, bioremediation, and biocatalysis . The enzyme’s ability to catalyze oxidative reactions makes it a valuable tool in these applications, and ongoing research aims to optimize its production and expand its use in biotechnological solutions .
