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SRP2152

Sigma-Aldrich

HIV Protease, His tagged,recombinant from HIV-1

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

Sinonimo/i:

HIV_retropepsin_like, Retropepsins, cd05482, pepsin-like aspartate proteases

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10 μG
490,00 €

490,00 €


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Cambia visualizzazione
10 μG
490,00 €

About This Item

Codice UNSPSC:
12352204
NACRES:
NA.26

490,00 €


Per informazioni sulla disponibilità, contatta il Servizio Clienti.

Origine biologica

human immunodeficiency virus 1

Ricombinante

expressed in E. coli

Saggio

≥85% (SDS-PAGE)

Stato

frozen liquid

PM

~11.9 kDa

Confezionamento

pkg of 10 μg

Condizioni di stoccaggio

avoid repeated freeze/thaw cycles

Concentrazione

200 μg/mL

Colore

colorless to clear

N° accesso NCBI

N° accesso UniProt

Condizioni di spedizione

dry ice

Temperatura di conservazione

−70°C

Categorie correlate

Applicazioni

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.[1]

Azioni biochim/fisiol

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.

Sequenza

PQITLWQRPL VTIKIGGQLK EALLDTGADD TVLEEMSLPG RWKPKMIGGI GGFIKVRQYD QILIEICGHK AIGTVLVGPT PVNIIGRNLL TQIGCTLNF

Stato fisico

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

Nota sulla preparazione

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.

Codice della classe di stoccaggio

10 - Combustible liquids

Classe di pericolosità dell'acqua (WGK)

WGK 1

Punto d’infiammabilità (°F)

Not applicable

Punto d’infiammabilità (°C)

Not applicable


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Noninvasive high-throughput single-cell analysis of HIV protease activity using ratiometric flow cytometry.
Gaber R
Sensors (Basel, Switzerland), 13, 16330-16346 (2013)
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 =

Domande

Recensioni

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