Hepatitis C Virus NS5, Recombinant (HCV) (Biotin)

The hepatitis C virus (HCV) NS5A gene product is a phosphorylated 56-58kD nonstructural protein that displays a multitude of activities related to enhancement of viral pathogenesis. Although associated with other viral encoded proteins as part of the viral replicase complex positioned on the cytoplasmic side of the endoplasmic reticulum, a role for NS5A in viral replication has not been defined. Truncated versions of NS5A can act as transcriptional activators, while other recently characterized interactions of NS5A with cellular proteins indicate its pleiotropic role in HCV-host interactions. It has been shown that NS5B is a membrane-associated protein, which contains a C-terminal domain comprising 21 hydrophobic amino acids that is responsible for membrane anchorage. NS5B may form a complex with cellular proteins or other HCV nonstructural proteins, including NS3, the viral protease and helicase; NS4A, a cofactor of NS3 protease activity; and NS5A, a phosphoprotein containing a putative interferon sensitivity region. Although the HCV replication mechanism is not clearly understood, the essential role of NS5B polymerase in the HCV replication and infection process has been demonstrated in chimpanzees. Accordingly, it has been viewed as an attractive target for antiviral intervention. It has been shown that NS5B is a membrane-associated protein, which contains a C-terminal domain comprising 21 hydrophobic amino acids that is responsible for membrane anchorage. NS5B may form a complex with cellular proteins or other HCV nonstructural proteins, including NS3, the viral protease and helicase; NS4A, a cofactor of NS3 protease activity; and NS5A, a phosphoprotein containing a putative interferon sensitivity region. Although the HCV replication mechanism is not clearly understood, the essential role of NS5B polymerase in the HCV replication and infection process has been demonstrated in chimpanzees. Accordingly, it has been viewed as an attractive target for antiviral intervention. \n\nApplications: Suitable for use in ELISA, Western Blot. Other applications not tested.\n\nRecommended Dilutions:\nOptimal dilutions to be determined by researcher.\n\nStorage and Stability:\nMay be stored at 4 degrees C for short-term only. For long-term storage, store at -20 degrees C. Aliquots are stable for at least 6 months at -20 degrees C. For maximum recovery of product, centrifuge the original vial after thawing and prior to removing the cap. Further dilutions can be made in assay buffer.

Prices direct from United States Biological

Quick response times

Exclusive Biosave savings/discounts

SPECIFICATIONS

Catalog Number

H1920-27C1

Size

100ug

Applications

ELISA, WB

Conjugates

Biotin

Form

Supplied as a liquid in 25mM Tris-HCl, 1mM EDTA, 1.5M urea, 50% glycerol. Labeled with Biotin.

Purity

Chromatographically purified ((same/more than) 95% by RP-HPLC, FPLC, or reducing/non-reducing SDS-PAGE Silver Stain).

References

1. Summa, V., Petrocchi, A., Taliani, M., Pace, P.: HCV NS5b RNA-dependent RNA polymerase inhibitors: from alpha,gamma-diketoacids to 4,5-dihydroxypyrimidine- or 3-methyl-5-hydroxypyrimidinonecarboxylic acids. Design and synthesis. J. Med. Chem. 47(22): 5336-9 (2004, Oct 21). 2. Gong, G.Z., Jiang, Y.F., Lai, L.Y.: HCV NS5A abrogates p53 protein function by interfering with p53-DNA binding. World J. Gastroenterol. 10(15): 2223-7 (2004, Aug 1). 3. Othman, S.B., Trabelsi, A., Bouzgarrou, N., Pozzetto, B.: Evaluation of a prototype HCV NS5b assay for typing strains of hepatitis C virus isolated from Tunisian haemodialysis patients. J. Virol. Methods 119(2): 177-81 (2004, Aug). 4. Pace, P., Nizi, E., Pesci, S., Summa, V.: The monoethyl ester of meconic acid is an active site inhibitor of HCV NS5B RNA-dependent RNA polymerase. Bioorg. Med. Chem. Lett. 14(12): 3257-61 (2004, Jun 21). 5. Goh, P.Y., Tan, Y.J., Tan, Y.H.: Cellular RNA helicase p68 relocalization and interaction with the hepatitis C virus (HCV) NS5B protein and the potential role of p68 in HCV RNA replication. J. Virol. 78(10): 5288-98 (2004, May). 6. Chan, L., Pereira, O., Das, S.K., Siddiqui, A., L'Heureux, L.: Discovery of thiophene-2-carboxylic acids as potent inhibitors of HCV NS5B polymerase and HCV subgenomic RNA replication. Part 2: tertiary amides. Bioorg. Med. Chem. Lett. 14(3): 797-800 (2004, Feb 9). 7. Kalliampakou, K.I., Kalamvoki, M., Mavromara, P.: Hepatitis C virus (HCV) NS5A protein downregulates HCV IRES-dependent translation. J. Gen. Virol. 86(Pt 4): 1015-25 (2005, Apr). 8. Yeh, C.T., Chang, M.H., Shyu, W.C., Chang, M.L., Yang, P.Y., Tsao, M.L., Lai, H.Y.: Characterization of a HCV NS5A protein derived from a patient with hepatoma. Biochem. Biophys. Res. Commun. 327(2): 516-22 (2005, Feb 11). 9. Beaulieu, P.L., Tsantrizos, Y.S.: Inhibitors of the HCV NS5B polymerase: new hope for the treatment of hepatitis C infections. Curr. Opin. Investig. Drugs 5(8): 838-50 (2004, Aug). 10. Gopalsamy, A., Lim, K., Ciszewski, G., Park, K., Ellingboe, J.W., Bloom, J., Insaf, S., Upeslacis, J., Mansour, T.S., Krishnamurthy, G., Damarla, M., Pyatski, Y., Ho, D., Howe, A.Y., Orlowski, M., Feld, B., O'Connell, J.: Discovery of pyrano[3,4-b]indoles as potent and selective HCV NS5B polymerase inhibitors. J. Med. Chem. 47(26): 6603-8 (2004, Dec 16). 11. Yannopoulos, C.G., Xu, P., Ni, F., Chan, L., Pereira, O.Z., Reddy, T.J., Das, S.K., Poisson, C., Nguyen-Ba, N., Turcotte, N., Proulx, M., Halab, L., Wang, W., Bedard, J., Morin, N., Hamel, M., Nicolas, O., Bilimoria, D., L'Heureux, L., Bethell, R., Dionne, G.: HCV NS5B polymerase-bound conformation of a soluble sulfonamide inhibitor by 2D transferred NOESY. Bioorg. Med. Chem. Lett. 14(21): 5333-7 (2004, Nov 1).

Additional Info

Immunoreactive with sera of HCV-infected individuals. Minimal specificity problems.