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SRP2152

Sigma-Aldrich

HIV Protease, His tagged,recombinant from HIV-1

recombinant, expressed in E. coli, ≥85% (SDS-PAGE)

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Synonym(s):
HIV_retropepsin_like, Retropepsins, cd05482, pepsin-like aspartate proteases
NACRES:
NA.26

biological source

human immunodeficiency virus 1

recombinant

expressed in E. coli

Assay

≥85% (SDS-PAGE)

form

frozen liquid

mol wt

~11.9 kDa

packaging

pkg of 10 μg

storage condition

avoid repeated freeze/thaw cycles

concentration

200 μg/mL

color

colorless to clear

NCBI accession no.

UniProt accession no.

shipped in

dry ice

storage temp.

−70°C

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This Item
SRP2155SRP2154SRP2153
recombinant

expressed in E. coli

recombinant

expressed in E. coli

recombinant

expressed in E. coli

recombinant

expressed in E. coli

assay

≥85% (SDS-PAGE)

assay

≥80% (SDS-PAGE)

assay

≥80% (SDS-PAGE)

assay

≥80% (SDS-PAGE)

form

frozen liquid

form

frozen liquid

form

frozen liquid

form

frozen liquid

mol wt

~11.9 kDa

mol wt

~22.7 kDa

mol wt

~22.7 kDa

mol wt

~22.7 kDa

packaging

pkg of 10 μg

packaging

pkg of 10 μg

packaging

pkg of 10 μg

packaging

pkg of 10 μg

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.

Sequence

PQITLWQRPL VTIKIGGQLK EALLDTGADD TVLEEMSLPG RWKPKMIGGI GGFIKVRQYD QILIEICGHK AIGTVLVGPT PVNIIGRNLL TQIGCTLNF

Physical form

Clear and colorless frozen liquid solution
Formulated in 20mM Mes buffer, pH6, 500mM KCl, 20% glycerol.

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.

Storage Class Code

10 - Combustible liquids

WGK

WGK 1

Flash Point(F)

Not applicable

Flash Point(C)

Not applicable


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C Peng et al.
Journal of virology, 63(6), 2550-2556 (1989-06-01)
It is generally believed that the gag gene product of human immunodeficiency virus type 1 (HIV-1) is processed into several core proteins by a virus-specific protease. We used deletion mutation analysis to study the role of HIV-specific protease in the
K C Chou et al.
Proteins, 24(1), 51-72 (1996-01-01)
Based on the sequence-coupled (Markov chain) model and vector-projection principle, a discriminant function method is proposed to predict sites in protein substrates that should be susceptible to cleavage by the HIV-1 protease. The discriminant function is defined by delta =
Noninvasive high-throughput single-cell analysis of HIV protease activity using ratiometric flow cytometry.
Gaber R
Sensors (Basel, Switzerland), 13, 16330-16346 (2013)

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