ns2

Expression system: Baculovirus Insect Cells
Length: 1-278, Full Length
Activity: Not Tested

Expression system: E. coli
Length: 1-278, Full Length
Activity: Not Tested

Expression system: HEK293 Cells
Length: 1-278, Full Length
Activity: Not Tested

Expression system: E. coli
Length: 1-277, Full Length
Activity: Not Tested

Expression system: E. coli
Length: 1-278, Full Length
Activity: Not Tested

Expression system: Baculovirus Insect Cells
Length: 1-278, Full Length
Activity: Not Tested

Expression system: Baculovirus Insect Cells
Length: 1-278, Full Length
Activity: Not Tested

Expression system: E. coli
Length: 1-278, Full Length
Activity: Not Tested

Expression system: Baculovirus Insect Cells
Length: 1-278, Full Length
Activity: Not Tested

Expression system: E. coli
Length: 1-90, Full Length
Activity: Not Tested

Expression system: Baculovirus Insect Cells
Length: 1-278, Full Length
Activity: Not Tested

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.

Influenza A H1N1 (A swine Guangxi NS2176 2012) Neuraminidase NA Protein (His) is expressed in HEK293 mammalian cells with His tag. The predicted molecular weight is 50.5 kDa and the accession number is A0A075ESB5.

Expression system: E. coli
Length: 1-122, Full Length
Activity: Not Tested

The NS1 Influenza protein is created by the internal protein-encoding, linear negative-sense, single-stranded RNA, NS gene segment and which also codes for the nuclear export protein or NEP, formerly referred to as the NS2 protein, which mediates the export of vRNPs. The non-structural (NS1) protein is found in Influenzavirus A, Influenzavirus B, and Influenzavirus C. The non-structural (NS1) protein of the highly pathogenic avian H5N1 viruses circulating in poultry and waterfowl in Southeast Asia is currently believed to be responsible for the enhanced virulence of the strain. The Non-structural (NS1) protein of influenza A virus is a non-essential virulence factor that has multiple accessory functions during viral infection. The major role ascribed to NS1 has been its inhibition of host immune responses, especially the limitation of both interferon (IFN) production and the antiviral effects of IFN-induced proteins, such as dsRNA-dependent protein kinase R (PKR) and 2'5'-oligoadenylate synthetase (OAS) RNase L. Non-structural (NS1) protein is a non-structural protein of the influenza A virus, which could only be expressed when cells are infected. The effect of NS1 protein on the host cell is still not clear. Not only could NS1 remarkably affect metabolism, but it could also slow down cell proliferation by blocking the cell cycle. Non-structural (NS1) protein may lead to the development of novel antiviral drugs, and the use of oncolytic influenza A viruses as potential anti-cancer agents.