PADI4_3

PADI4_3 binds specifically and with high affinity to the active conformation of recombinant PADI4 in the calcium-bound state (K_D = 2.7 nM), and does not bind to the calcium-free inactive form or the active form with a blocked active site of this enzyme^[1].
PADI4_3 (0.0003-100 μM) potently inhibits the activity of recombinant PADI4 in vitro, with an IC₅₀ of 56 nM^[1].
PADI4_3 (200 nM-100 μM; 4 h) exhibits cell permeability in HaLo-GFP-mito HeLa cells, with a CP₅₀ of 1.4 μM at 37°C, and enters cells via an active transport mechanism^[1].
PADI4_3 (0.1-1 μM; 3 h) inhibits PADI4 activity in mES cells stably expressing hPADI4, with an EC₅₀ of 0.2 μM. At a concentration of 1 μM, it achieves complete inhibition without cytotoxicity^[1].
PADI4_3 (50 μM; 60 min pre-incubation) reduces the citrullination level of histone H3 and the formation of neutrophil extracellular traps (NETosis) in human primary peripheral blood neutrophils stimulated by calcium ionophores, while the inactive control peptide PADI4_3i has no effect on these endpoints^[1].
PADI4_3 potently inhibits the activity of recombinant PADI4 (IC₅₀ = 56 nM) with high selectivity; it shows no inhibitory effect on other human PADI isozymes or mouse PADI4 even at concentrations up to 100 μM^[2].

MedChemExpress (MCE) has not independently confirmed the accuracy of these methods. They are for reference only. Further protocols information, click here.