IMG-EN-AS-72028-5-01.jpg
Protein

HIV-1 protease, recombinant - 5 µg

$432.00
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  • Cat.Number : AS-72028-5
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The 10~12 kDa aspartic protease of human immunodeficiency virus-1 (HIV-1), active only when it forms a homodimer, is required for the post-translational cleavage of the precursor polyproteins, Gag, Gag-Pol, Pol, and Nef. Since the cleavages of precursors are essential for the maturation of HIV infectious particles, this protease is one of the key targets for developing anti-AIDS drugs

The recombinant HIV-1 protease (wild type, NCBI accession: NC_001802) contains the 99 amino acid sequence as reported by Schneider, et al. (Cell 54, 363;1988) with 6x His-tag at its C-terminal. HIV-1 protease activity can be measured using enzymatic assay with FRET substrates.

Specifications

Chemistry
Molecular Mass/ Weight
  • 12 kDa
Modification
Conjugation
  • Unconjugated
Quantity & Purity
Concentration
  • 0.2 mg/ml
Purity
  • ≥95% by SDS-PAGE
Storage & stability
Form
  • In solution
Storage Conditions
  • Store at -80°C. Avoid repeated freeze-thaw cycles.
Activity
Application
Biomarker Target
Unit definition
  • One unit of protease hydrolyzes 1 picomole of the DABCYL/EDANS substrate in SensoLyte™ 490 HIV Protease Assay Kits (AnaSpec Cat# 71127) per min at pH 4.7 at 25°C.
Specificity
  • Recombinant HIV-1 protease (wild type, NCBI accession: NC_001802) containing 99 amino acids
Research Area
Sub-category Research Area
Usage
  • Research use
Source
Host
Source / Species
  • Human Immunodeficiency Virus

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References

Enzymatic activity of a synthetic 99 residue protein corresponding to the putative HIV-1 protease

Cell . 1988 Jul 29 ; 54(3) 363 | DOI : https://doi.org/10.1016/0092-8674(88)90199-7

  • J. Schneider
  • SBH. Kent

Human immunodeficiency virus has an aspartic-type protease that can be inhibited by pepstatin A

PNAS USA . 1988 Sep 01 ; 85(18) 6612 | DOI : https://doi.org/10.1073/pnas.85.18.6612

  • S. Seelmeier
  • et al