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Protein arginine deiminase 4 (PAD4) catalyzes the conversion of arginine residues to citrulline within cellular protein substrates, resulting in the loss of a positive charge, which can alter protein structure and/or function.1 It is expressed in neutrophils, as well as a variety of tissues, including the brain, liver, lung, and kidney.1,2,3 PAD4 has a key role in NETosis, a lytic form of cell death characterized by the release of neutrophil extracellular traps (NETs).1 Upon neutrophil activation, PAD4 translocates to the nucleus where it citrullinates histones, initiating chromatin decondensation and the release of NETs.2,4,5 A missense mutation in PADI4 leading to a leucine-to-methionine mutation at position 117 (PAD4L117M) is associated with increased susceptibility to rheumatoid arthritis.6,7,8 Cayman’s PAD4 (L117M mutant; human, recombinant) protein can be used for enzyme activity assay and Western blot (WB) applications.
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