IMG-EN-AS-60635-01.jpg
Peptides

HIV Substrate, HiLyte™ Fluor 488 - 0.1 mg

$154.00
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  • Cat.Number : AS-60635
  • Availability :
    In production

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Ths is a HiLyte Fluor labeled HIV protease substrate I, GABA-Ser-Gln-Asn-Tyr-Pro-Ile-Val-Gln-EDANS. The peptide sequence is derived from the native p17/p24 cleavage site on HIV precursor polyprotein Prgag for HIV-1 protease. Cleavage of HIV precursor polyproteins is essential for the maturation of the infectious virus and hence the protease has become a major target for developing anti-AIDS drugs. The peptide substrate is widely used for the continuous assay for HIV protease activity. The QXL/488 pair offers better sensitivity in detection at a higher wavelength with less background interference. (Excitation/Emission = 490 nm/520 nm).

Specifications

Chemistry
Sequence one letter code
  • QXL®520-GABA-SQNYPIVQ-K(HiLyte™ Fluor 488)-NH2
Sequence three letter code
  • QXL® 520-GABA-Ser-Gln-Asn-Tyr-Pro-Ile-Val-Gln-Lys(Hilyte™ Fluor 488)-NH2
Molecular Mass/ Weight
  • 2008.2
Properties
Absorbance (nm)
  • 490
Emission (nm)
  • 520
Modification
Conjugation type
  • Double dyes
Modification Name
Conjugation
  • Conjugated
Quantity & Purity
Purity
  • Peak Area by HPLC ≥95%
Storage & stability
Form
  • Lyophilized
Storage Conditions
  • - 20 °C Protected from light
Activity
Application
Biomarker Target
Detection Method
Research Area
Sub-category Research Area
Usage
  • Research use
Source
Source / Species
  • HIV

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References

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

Proc Natl Acad Sci USA . 1988 Sep 01 ; 85(18) 6612 | DOI : 10.1073/pnas.85.18.6612.

  • S. Seelmeier
  • et al

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

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

  • J. Schneider
  • SBH. Kent

Development and evaluation of a phenotypic assay monitoring resistance formation to protease inhibitors in HIV-1-infected patients

J Virol Methods . 2003 May 01 ; 109(2) 143 | DOI : https://doi.org/10.1016/S0166-0934(03)00065-X

  • H. Gehringer
  • et al