Leader cysteine autoprotease that cleaves itself from the nascent polyprotein during translation of the viral mRNA. Once released, plays a role in the inhibition of host innate immune response by interacting with host IRF3 and inducing its proteasomal degradation.; Packages viral RNA to form a viral nucleocapsid and thereby protects viral RNA. Plays also a role in transcription regulation. Protects the incoming virus against IFN-induced effectors.; Initial binding to target cell probably involves interaction of E(rns) with glycosaminoglycans.; E1 and/or E2 are probably responsible of cell attachment with CD46 and subsequent fusion after internalization of the virion by endocytosis.; E1 and/or E2 are probably responsible of cell attachment with CD46 and subsequent fusion after internalization of the virion by endocytosis.; Plays an essential role in the virus replication cycle by acting as a viroporin. Forms ion conductive pores, which alters the cell permeability allowing the transport of ions and other small molecules. Forms a leader sequence to properly orient NS2 in the membrane.; Uncleaved NS2-3 is required for production of infectious virus.; Plays a role in the regulation of viral RNA replication.; Multifunctional protein that contains an N-terminal protease and a C-terminal helicase, playing essential roles in viral polyprotein processing and viral genome replication. The chymotrypsin-like serine protease activity utilizes NS4A as an essential cofactor and catalyzes the cleavage of the polyprotein leading to the release of NS4A, NS4B, NS5A, and NS5B. Interacts with NS5B to enhance RNA-dependent RNA polymerase activity.; Acts as a cofactor for the NS3 protease activity.; Induces a specific membrane alteration that serves as a scaffold for the virus replication complex.; Replicates the viral (+) and (-) genome.
Pack Size | Availability | Price/USD | Quantity |
---|---|---|---|
20 μg | 20 days | $ 360.00 | |
100 μg | 20 days | $ 678.00 | |
1 mg | 20 days | $ 2,300.00 |
Description | Leader cysteine autoprotease that cleaves itself from the nascent polyprotein during translation of the viral mRNA. Once released, plays a role in the inhibition of host innate immune response by interacting with host IRF3 and inducing its proteasomal degradation.; Packages viral RNA to form a viral nucleocapsid and thereby protects viral RNA. Plays also a role in transcription regulation. Protects the incoming virus against IFN-induced effectors.; Initial binding to target cell probably involves interaction of E(rns) with glycosaminoglycans.; E1 and/or E2 are probably responsible of cell attachment with CD46 and subsequent fusion after internalization of the virion by endocytosis.; E1 and/or E2 are probably responsible of cell attachment with CD46 and subsequent fusion after internalization of the virion by endocytosis.; Plays an essential role in the virus replication cycle by acting as a viroporin. Forms ion conductive pores, which alters the cell permeability allowing the transport of ions and other small molecules. Forms a leader sequence to properly orient NS2 in the membrane.; Uncleaved NS2-3 is required for production of infectious virus.; Plays a role in the regulation of viral RNA replication.; Multifunctional protein that contains an N-terminal protease and a C-terminal helicase, playing essential roles in viral polyprotein processing and viral genome replication. The chymotrypsin-like serine protease activity utilizes NS4A as an essential cofactor and catalyzes the cleavage of the polyprotein leading to the release of NS4A, NS4B, NS5A, and NS5B. Interacts with NS5B to enhance RNA-dependent RNA polymerase activity.; Acts as a cofactor for the NS3 protease activity.; Induces a specific membrane alteration that serves as a scaffold for the virus replication complex.; Replicates the viral (+) and (-) genome. |
Species | BVDV |
Expression System | E. coli |
Tag | N-terminal 10xHis-tagged |
Accession Number | Q01499 |
Synonyms | Genome polyprotein |
Amino Acid | MELITNELLYKTYKQKPVGVEEPVYDQAGNPLFGERGAIHPQSTLKLPHKRGERNVPTSLASLPKRGDCRSGNSKGPVSGIYLKPGPLFYQDYKGPVYHRAPLELFEEGSMCETTKRIGRVTGSDGKLYHIYICIDGCITVKSATRSHQRVLRWVHNRLDCPLWVTSC Note: The complete sequence including tag sequence, target protein sequence and linker sequence could be provided upon request. |
Construction | 1-168 aa |
Protein Purity | > 85% as determined by SDS-PAGE. |
Molecular Weight | 25.0 kDa (predicted) |
Formulation | Tris-based buffer,50% glycerol |
Reconstitution | A hardcopy of COA with reconstitution instructions is sent along with the products. Please refer to it for detailed information. |
Stability & Storage |
Generally, the shelf life of liquid form is 6 months at -20°C/-80°C. The shelf life of lyophilized form is 12 months at -20°C/-80°C. |
Shipping |
In general, recombinant proteins are provided as lyophilized powder which are shipped at ambient temperature. Bulk packages of recombinant proteins are provided as frozen liquid. They are shipped out with blue ice unless customers require otherwise. |
Research Background | Leader cysteine autoprotease that cleaves itself from the nascent polyprotein during translation of the viral mRNA. Once released, plays a role in the inhibition of host innate immune response by interacting with host IRF3 and inducing its proteasomal degradation.; Packages viral RNA to form a viral nucleocapsid and thereby protects viral RNA. Plays also a role in transcription regulation. Protects the incoming virus against IFN-induced effectors.; Initial binding to target cell probably involves interaction of E(rns) with glycosaminoglycans.; E1 and/or E2 are probably responsible of cell attachment with CD46 and subsequent fusion after internalization of the virion by endocytosis.; E1 and/or E2 are probably responsible of cell attachment with CD46 and subsequent fusion after internalization of the virion by endocytosis.; Plays an essential role in the virus replication cycle by acting as a viroporin. Forms ion conductive pores, which alters the cell permeability allowing the transport of ions and other small molecules. Forms a leader sequence to properly orient NS2 in the membrane.; Uncleaved NS2-3 is required for production of infectious virus.; Plays a role in the regulation of viral RNA replication.; Multifunctional protein that contains an N-terminal protease and a C-terminal helicase, playing essential roles in viral polyprotein processing and viral genome replication. The chymotrypsin-like serine protease activity utilizes NS4A as an essential cofactor and catalyzes the cleavage of the polyprotein leading to the release of NS4A, NS4B, NS5A, and NS5B. Interacts with NS5B to enhance RNA-dependent RNA polymerase activity.; Acts as a cofactor for the NS3 protease activity.; Induces a specific membrane alteration that serves as a scaffold for the virus replication complex.; Replicates the viral (+) and (-) genome. |
bottom
Please read the User Guide of Recombinant Proteins for more specific information.
Bovine viral diarrhea virus (strain SD-1) Genome polyprotein (E. coli, His) Genome polyprotein recombinant recombinant-proteins proteins protein