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HIV-2 Protease E.coli

  • Regulatory status:RUO
  • Type:Active protein
  • Source:E. coli
  • Species:Human Immunodeficiency Virus 2
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Cat. No. Size Price


RH2P0001 0.1 mg
PubMed Product Details
Technical Data

Type

Active protein

Description

Total 99 AA. MW: 10.7 kDa (monomer), protein active as dimer

Amino Acid Sequence

PQFSLWKRPVVTAHIEGQPVEVLLDTGADDSIVAGIELGSNYSPKIVGGIGGFINTKEYKNVEIEVLNKRVRATIMTGDTPINIFGRNILASLGMSLNL

Source

E. coli

Purity

Purity as determined by densitometric image analysis: >95%

SDS-PAGE Gel

14% SDS-PAGE separation of Human HIV-2 Protease
1. M.W. marker – 10, 20, 30, 40, 60, 80 kDa
2. reduced and heated sample, 2.5 μg/lane

Formulation

20 mM Tris, 20 mM MES, 200 mM NaCl, 10% glycerol, 1 mM EDTA, 0.5 mM DTT, 0.05% PEG 8000, pH 7.0 – filtered (0.4 μm), frozen

Reconstitution

Defrost at ambient temperature.

Applications

Kinetic studies, Inhibitor screening, Crystallography

Shipping

On ice. Upon receipt, store the product at the temperature recommended below.

Storage/Expiration

Store protein at –80°C. Protein remains stable until the expiry date when stored at –80°C. Avoid repeated freezing/thawing cycles.

Quality Control Test

SDS PAGE to determine purity of the protein.
Active site titration by tightly binding inhibitor.

Note

Km = 740 μM Kcat = 3 s-1 Kcat /Km = 4.1 mM-1 s-1 with peptide substrate ATLNFPISPW

Summary

Research topic

Others

Summary

Retroviral protease from HIV-2 virus is an enzyme important in the life cycle of the virus. It is expressed in the infected cells as a part of Gag-Pol polyprotein from which it is autocatalytycaly released after formation of immature viral particle. The enzyme subsequently cleaves the other parts of viral polyproteins causing the maturation of the virus. In HIV-infected patients the enzyme is a subject of intensive mutagenesis and mutants resistant to applied medcines are produced as a consequence of the selection pressure. HIV-2 protease is active as a homodimer.

Summary References (3)

References to HIV-2 Protease

  • Kovalevsky AY, Louis JM, Aniana A, Ghosh AK, Weber IT. Structural evidence for effectiveness of darunavir and two related antiviral inhibitors against HIV-2 protease. J Mol Biol. 2008 Dec 5;384 (1):178-92
  • Rose JR, Salto R, Craik CS. Regulation of autoproteolysis of the HIV-1 and HIV-2 proteases with engineered amino acid substitutions. J Biol Chem. 1993 Jun 5;268 (16):11939-45
  • Tong L, Pav S, Pargellis C, Do F, Lamarre D, Anderson PC. Crystal structure of human immunodeficiency virus (HIV) type 2 protease in complex with a reduced amide inhibitor and comparison with HIV-1 protease structures. Proc Natl Acad Sci U S A. 1993 Sep 15;90 (18):8387-91
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