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Assay-kits

SensoLyte® 520 HIV Protease Assay Kit Fluorimetric - 1 kit

$582.00
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  • Cat.Number : AS-71147
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The SensoLyte® 520 HIV Assay Kit uses a new FRET peptide substrate that incorporates HiLyte™ Fluor 488 (fluorophore) and QXL™ 520 (quencher) for continuous measurement of enzyme activities. In the intact FRET peptide, the fluorescence of HiLyte™ Fluor 488 is quenched by QXL™ 520. Upon cleavage of the FRET peptide by HIV protease, the fluorescence of HiLyte™ Fluor 488 is recovered and can be continuously monitored at excitation/emission = 490 nm/520 nm. With superior fluorescence quantum yield and longer emission wavelength, this HiLyte™ Fluor 488/QXL™ 520-based FRET peptide shows less interference from autofluorescence of test compounds and cellular components, thus providing better assay sensitivity. The assays are performed in a convenient 96-well or 384-well microplate format.

Specifications

Packaging
Kits components
  • Component A: HIV-1 protease FRET substrate: 120 µL Component B: HiLyte Fluor™488, fluorescence reference standard Ex/Em=490 nm/520 nm: 100 µM, 5 µL Component C: Pepstatin A, a characterized HIV-1 protease inhibitor: 27.4 µg powder Component D: 2X Assay buffer 20 mL Component E: Stop solution: 10 mL Component F: DMSO: 50 µL Component G: DTT: 1 M, 150 µL
Properties
Absorbance (nm)
  • 490
Emission (nm)
  • 520
Storage & stability
Storage Conditions
  • Store all components at -20°C. Components E and F can be stored at room temperature for convenience. Protect Components A and B from light.
Activity
Application
Biomarker Target
Detection Method
Research Area
Sub-category Research Area
Usage
  • Research use

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Citations

Screening of HIV-1 protease using a combination of an ultra-high-throughput fluorescent-based assay and RapidFire mass spectrometry

J Biomol Screen . 2015 Feb 13 ; 20(5) 606 | DOI : 10.1177/1087057115570838

  • J. Meng

Synthesis of dammarane-type triterpene derivatives and their ability to inhibit HIV and HCV proteases

Bioorg Med Chem . 2009 Mar 14 ; 17(8) 3003 | DOI : 10.1016/j.bmc.2009.03.019

  • Y. Wei