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Pathways Recommended: Metabolic Enzyme/Protease
Results for "

retroviral protease

" in MedChemExpress (MCE) Product Catalog:

5

Inhibitors & Agonists

1

Fluorescent Dye

2

Peptides

1

Isotope-Labeled Compounds

Cat. No. Product Name Target Research Areas Chemical Structure
  • HY-D1080
    EDANS
    1 Publications Verification

    1,5-EDANS

    Fluorescent Dye Others
    EDANS (1,5-EDANS) is a novel and quenched fluorogenic substrate for assaying retroviral protease by resonance energy transfer (RET) .
    EDANS
  • HY-D1080R

    1,5-EDANS (Standard)

    Fluorescent Dye Others
    EDANS (1,5-EDANS) (Standard) is an analytical standard for EDANS. This product is intended for research and analytical applications. EDANS (1,5-EDANS) is a novel quenched fluorogenic substrate for the analysis of retroviral proteases by resonance energy transfer .
    EDANS (Standard)
  • HY-120757

    Virus Protease Others
    LP-130 is a statin-based inhibitor that is a universal inhibitor with nanomolar inhibitory activity against all tested retroviral proteases. Crystal structure studies of its binding to different retroviral proteases have shown that it can adapt to different active site regions to achieve inhibition.
    LP-130
  • HY-176305S

    Isotope-Labeled Compounds Neurological Disease
    Neurofilament, U- 15N is the 15N-labeled Neurofilament.
    Neurofilament, U-15N
  • HY-P5415

    HIV Others
    DABCYL-GABA-Ser-Gln-Asn-Tyr-Pro-Ile-Val-Gln-EDANS is a biological active peptide. (DABCYL-GABA-Ser-Gln-Asn-Tyr-Pro-Ile-Val-Gln-EDANS is also called HIV protease substrate I in some literature. It is widely used for the continuous assay for HIV protease activity. The 11-kD protease (PR) encoded by the human immunodeficiency virus 1 (HIV-1) is essential for the correct processing of viral polyproteins and the maturation of infectious virus, and is therefore a target for the design of selective acquired immunodeficiency syndrome (AIDS) therapeutics. The FRET-based fluorogenic substrate is derived from a natural processing site for HIV-1 PR. Incubation of recombinant HIV-1 PR with the fluorogenic substrate resulted in specific cleavage at the Tyr-Pro bond and a time-dependent increase in fluorescence intensity that is linearly related to the extent of substrate hydrolysis. The fluorescence quantum yields of the HIV-1 PR substrate in the FRET assay increased by 40.0- and 34.4-fold, respectively, per mole of substrate cleaved. Because of its simplicity and precision in the determination of reaction rates required for kinetic analysis, this substrate offers many advantages over the commonly used HPLC or electrophoresis-based assays for peptide substrate hydrolysis by retroviral PRs. Abs/Em = 340nm/490nm.)
    DABCYL-GABA-Ser-Gln-Asn-Tyr-Pro-Ile-Val-Gln-EDANS

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