Introduction The HIV-1 core consists of a viral genome housed within a conical viral capsid that is generated during virion maturation. Human immunodeficiency virus type 1 (HIV-1) matures after the viral protease processes (1) the Gag and Pol polyproteins at 10 substrate locations (2, 3). The protease of HIV-1 is an aspartic protease and is functional only as a dimer; dimerization results in the formation of a binding cleft in which each of the two catalytic aspartic acids in which each monomer contributes each of the 2 catalytic aspartic acids. Because the protease is active only as a dimer, two of the GagPol precursors must themselves dimerize during virus assembly so that their protease domains can dimerize, become active, and process the precursors (4). Both the order and kinetics of cleavage as well as the extent of precursor processing appear to be critical steps in the generation of fully infectious, appropriately assembled viral particles (5-7). Inhibition of HIV-1 protease represents an important avenue for antiviral therapy (8). Currently available combination chemotherapy with reverse transcriptase inhibitors (RTIs) and protease inhibitors (PIs) for human immunodeficiency virus type 1 (HIV-1) infection and AIDS have been shown to suppress the replication of HIV-1 and extend the life expectancy of HIV-1-infected individuals (9).
Description The recombinant HIV-1 protease (wild type) contains the 99 amino acid sequence, with 6x His-tag at its C-terminal. Molecular weight is around 10-12 kDa, HIV protease active only when it forms a homodimer. Recombinant HIV Protease was expressed in an E.coli system and purified by an affinity chromatography in combination with FPLC chromatography. The purified recombinant protein is greater than 95% homogeneous based on SDS-PAGE Gel analysis.
Synonym HIV retropepsin like; Retropepsins; pepsin-like aspartate proteases; cd05482
Formulation and storage HIV protease is stored in 20mM Mes buffer, pH6, 500mM KCl, 20% glycerol. It lost 70% activity in 4°C for one week. Please keep in -20°C for long term storage. Freeze thaw cycle resistance.
Application One unit of HIV Protease hydrolyzes 1 picomole of a peptide (SQNYPIVQ) per minute at pH 4.7 at 25oC. 20-200ng is sufficient for an in vitro protease assay. HIV Protease can be applied in in vitro assay development and screening of protease inhibitors.
Reference 1. Peng, C., et al., 1989. J. Virol. 63:2550-2556. 2. Chou, K.-C., et al., 1996. Proteins 24:51-72 3. Henderson, L. E., et al., 1988. Alan R. Liss, New York, N.Y. 4. Navia, M. A., and B. M. McKeever. 1990. Ann. N. Y. Acad. Sci. 616:73-85. 5. Krausslich, H. G., et al., 1995. J. Virol. 69:3407-3419. 6. Mervis, R. J., et al., 1988. J. Virol. 62:3993-4002. 7. Pettit, S. C., et al., 1994. J. Virol. 68:8017-8027. 8. Temesgen, Z. 2001. Expert Opin. Pharmacother. 2:1239-1246. 9. Zhang, Y. M., et al., 1997. J. Virol. 71:6662-6670
DISCLAIMER
This products is recommended For RESEARCH USE ONLY and is Not qualified for Use in Diagnostic or Therapeutic Procedures.
