(S)-PFI-2 hydrochloride selectively inhibits the lysine methyltransferase SETD7, demonstrating approximately 500-fold higher potency compared to its (R) enantiomer. This compound operates via a unique mechanism that alters the catalytic functionality of SETD7, influencing the binding dynamics with substrate peptides and cofactor interactions. Its targeted inhibition positions (S)-PFI-2 as a valuable tool for investigating SETD7's role in various biological processes, including epigenetic regulation and cellular signaling pathways. This compound is particularly relevant for research applications focused on methylation dynamics and related therapeutics.
(S)-PFI-2 hydrochloride selectively inhibits the lysine methyltransferase SETD7, demonstrating approximately 500-fold higher potency compared to its (R) enantiomer. This compound operates via a unique mechanism that alters the catalytic functionality of SETD7, influencing the binding dynamics with substrate peptides and cofactor interactions. Its targeted inhibition positions (S)-PFI-2 as a valuable tool for investigating SETD7's role in various biological processes, including epigenetic regulation and cellular signaling pathways. This compound is particularly relevant for research applications focused on methylation dynamics and related therapeutics.
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