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Non-structural protein 2 (NS2) plays a crucial role in the hepatitis C virus (HCV) assembly. NS2 was predicted to be composed of three transmembrane (TM) segments. Hepatitis C virus (HCV) nonstructural protein 2 (NS2) is a hydrophobic, transmembrane protein that is required not only for NS2-NS3 cleavage but also for infectious virus production.NS2 protein is essential for hepatitis C virus (HCV) replication. NS2 protein was expressed and purified. Aptamers against NS2 protein were raised and antiviral effects of the aptamers were examined. The non-structural protein NS2, also called nuclear export protein, of influenza A virus contains a leucine-rich nuclear export signal that could guide viral ribonucleoproteins to cross the nuclear pore complex (NPC) and complete directional nucleocytoplasmic trafficking.
Pack Size | Price | Availability | Quantity |
---|---|---|---|
100 μg | $801 | 7-10 days |
Biological Activity | Activity testing is in progress. It is theoretically active, but we cannot guarantee it. If you require protein activity, we recommend choosing the eukaryotic expression version first. |
Description | Non-structural protein 2 (NS2) plays a crucial role in the hepatitis C virus (HCV) assembly. NS2 was predicted to be composed of three transmembrane (TM) segments. Hepatitis C virus (HCV) nonstructural protein 2 (NS2) is a hydrophobic, transmembrane protein that is required not only for NS2-NS3 cleavage but also for infectious virus production.NS2 protein is essential for hepatitis C virus (HCV) replication. NS2 protein was expressed and purified. Aptamers against NS2 protein were raised and antiviral effects of the aptamers were examined. The non-structural protein NS2, also called nuclear export protein, of influenza A virus contains a leucine-rich nuclear export signal that could guide viral ribonucleoproteins to cross the nuclear pore complex (NPC) and complete directional nucleocytoplasmic trafficking. |
Species | H1N1 |
Expression System | E. coli |
Tag | Tag Free |
Accession Number | P03508.1 |
Synonyms | NS2 Protein |
Construction | A DNA sequence encoding the influenza A H1N1 Virus (A/Puerto Rico/8/34/Mount Sinai) NS2 protein (P03508.1) (Met 1-Ile 121) was expressed, with a polyhistidine tag at the N-terminus. Predicted N terminal: Met 1 |
Protein Purity | > 95 % as determined by SDS-PAGE |
Molecular Weight | 14.4 kDa (predicted); 13 kDa (reducing conditions) |
Endotoxin | < 1.0 EU/μg of the protein as determined by the LAL method. |
Formulation | Lyophilized from a solution filtered through a 0.22 μm filter, containing 20 mM HEPES, 1 mM EDTA, pH 7.0.Typically, a mixture containing 5% to 8% trehalose, mannitol, and 0.01% Tween 80 is incorporated as a protective agent before lyophilization. |
Reconstitution | A Certificate of Analysis (CoA) containing reconstitution instructions is included with the products. Please refer to the CoA for detailed information. |
Stability & Storage | It is recommended to store recombinant proteins at -20°C to -80°C for future use. Lyophilized powders can be stably stored for over 12 months, while liquid products can be stored for 6-12 months at -80°C. For reconstituted protein solutions, the solution can be stored at -20°C to -80°C for at least 3 months. Please avoid multiple freeze-thaw cycles and store products in aliquots. |
Shipping | In general, Lyophilized powders are shipping with blue ice. |
Research Background | Non-structural protein 2 (NS2) plays a crucial role in the hepatitis C virus (HCV) assembly. NS2 was predicted to be composed of three transmembrane (TM) segments. Hepatitis C virus (HCV) nonstructural protein 2 (NS2) is a hydrophobic, transmembrane protein that is required not only for NS2-NS3 cleavage but also for infectious virus production.NS2 protein is essential for hepatitis C virus (HCV) replication. NS2 protein was expressed and purified. Aptamers against NS2 protein were raised and antiviral effects of the aptamers were examined. The non-structural protein NS2, also called nuclear export protein, of influenza A virus contains a leucine-rich nuclear export signal that could guide viral ribonucleoproteins to cross the nuclear pore complex (NPC) and complete directional nucleocytoplasmic trafficking. |
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