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Results for "

human MacroD2

" in MedChemExpress (MCE) Product Catalog:

3

Inhibitors & Agonists

1

Fluorescent Dye

1

Oligonucleotides

Cat. No. Product Name Target Research Areas Chemical Structure
  • HY-146248B

    Poly(ADP-ribose) Glycohydrolase (PARG) SARS-CoV Protease Activated Receptor (PAR) Metabolic Disease
    TFMU-ADPr diammonium is a selective reporter substrate of SARS-CoV-2 Macro1 (IC50=0.59 μM), with an excitation wavelength (λEx) of 385 nm, and an emission wavelength (λEm) of 502 nm (or 495 nm). TFMU-ADPr diammonium can also undergo enzymatic hydrolysis with Poly(ADP-ribose) Glycohydrolase (PARG) sourced from human, Tetrahymena thermophila and ADP-ribosylhydrolase 3 from human to release fluorophores, thereby directly reporting total poly (ADP-ribose) hydrolase activity. TFMU-ADPr diammonium binds to the ADPr-binding site of SARS-CoV-2 Macro1, and its TFMU moiety inserts into the narrow hydrophobic groove of this protein. TFMU-ADPr diammonium can thus be used to evaluate small-molecule inhibitors targeting PAR hydrolases under in vitro conditions, to investigate the regulatory mechanisms of ADP-ribosyl catabolic enzymes, or to detect PAR hydrolase activity in whole-cell lysate assays. TFMU-ADPr diammonium is also applicable to COVID-19-related research .
    TFMU-ADPr diammonium
  • HY-RS07946

    Small Interfering RNA (siRNA) Others

    MACROD2 Human Pre-designed siRNA Set A contains three designed siRNAs for MACROD2 gene (Human), as well as a negative control, a positive control, and a FAM-labeled negative control.

    MACROD2 Human Pre-designed siRNA Set A
    MACROD2 Human Pre-designed siRNA Set A
  • HY-146248

    SARS-CoV Poly(ADP-ribose) Glycohydrolase (PARG) Protease Activated Receptor (PAR) Infection
    TFMU-ADPr is a selective reporter substrate of SARS-CoV-2 Macro1 (IC50=0.59 μM), with an excitation wavelength (λEx) of 385 nm, and an emission wavelength (λEm) of 502 nm (or 495 nm). TFMU-ADPr can also undergo enzymatic hydrolysis with Poly(ADP-ribose) Glycohydrolase (PARG) sourced from human, Tetrahymena thermophila and ADP-ribosylhydrolase 3 from human to release fluorophores, thereby directly reporting total poly (ADP-ribose) hydrolase activity. TFMU-ADPr binds to the ADPr-binding site of SARS-CoV-2 Macro1, and its TFMU moiety inserts into the narrow hydrophobic groove of this protein. TFMU-ADPr can thus be used to evaluate small-molecule inhibitors targeting PAR hydrolases under in vitro conditions, to investigate the regulatory mechanisms of ADP-ribosyl catabolic enzymes, or to detect PAR hydrolase activity in whole-cell lysate assays. TFMU-ADPr is also applicable to COVID-19-related research .
    TFMU-ADPr

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