Non disponible en dehors du Royaume-Uni et de l'Irlande

Application

HIV Protease has been used in in vitro detection of HIV protease activity using FRET-HIV Sensor, a Förster resonance energy transfer-based HIV protease-sensitive sensor.

Biochem/physiol Actions

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 the Gag and Pol polyproteins at 10 substrate locations. 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 is contributed by one of the monomers. 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. 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. Inhibition of HIV-1 protease represents an important avenue for antiviral therapy. 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.

Physical form

Formulated in 20mM Mes buffer, pH6, 500mM KCl, 20% glycerol.

Clear and colorless frozen liquid solution

Preparation Note

Please keep in −20 °C for long term storage. It lost 70% activity in 4°C for one week. Freeze thaw cycle resistance.

Use a manual defrost freezer and avoid repeated freeze-thaw cycles. While working, please keep sample on ice.

Sequence

PQITLWQRPL VTIKIGGQLK EALLDTGADD TVLEEMSLPG RWKPKMIGGI GGFIKVRQYD QILIEICGHK AIGTVLVGPT PVNIIGRNLL TQIGCTLNF