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Influenza A H1N1 (A/Puerto Rico/8/34/Mount Sinai) Non-structural/NS2 Protein

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Influenza A H1N1 (A/Puerto Rico/8/34/Mount Sinai) Non-structural/NS2 Protein

Catalog No. TMPY-02285

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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Pack Size	Price	Availability	Quantity
100 μg	$801	7-10 days

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Biological Description

Biological Information	Testing in progress
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	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.
Protein Purity	> 95 % as determined by SDS-PAGE
Molecular Weight	14.4 kDa (predicted)
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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