TFMU-ADPr is a selective reporter substrate that targets the SARS-CoV-2 Macro1 protein, displaying an IC50 of 0.59 μM. This compound emits fluorescence at 502 nm (or 495 nm) upon enzymatic hydrolysis by Poly(ADP-ribose) Glycohydrolase (PARG) and ADP-ribosylhydrolase 3. TFMU-ADPr binds to the ADPr-binding site of Macro1, providing a robust method for assessing the activity of poly(ADP-ribose) hydrolases. Its applications extend to evaluating small-molecule inhibitors under in vitro conditions, investigating ADP-ribosyl catabolic enzyme mechanisms, and detecting PAR hydrolase activity in whole-cell lysates, making it a valuable tool for COVID-19-related research.
TFMU-ADPr is a selective reporter substrate that targets the SARS-CoV-2 Macro1 protein, displaying an IC50 of 0.59 μM. This compound emits fluorescence at 502 nm (or 495 nm) upon enzymatic hydrolysis by Poly(ADP-ribose) Glycohydrolase (PARG) and ADP-ribosylhydrolase 3. TFMU-ADPr binds to the ADPr-binding site of Macro1, providing a robust method for assessing the activity of poly(ADP-ribose) hydrolases. Its applications extend to evaluating small-molecule inhibitors under in vitro conditions, investigating ADP-ribosyl catabolic enzyme mechanisms, and detecting PAR hydrolase activity in whole-cell lysates, making it a valuable tool for COVID-19-related research.
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