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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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1. Peptidylarginine deiminase expression and activity in PAD2 knock-
2. Priming of neutrophils toward NETosis promotes tumor growth. Oncoimmunology 5(5), e1134073 (2016).
3. Protein arginine deiminase 4 (PAD4): Current understanding and future therapeutic potential. Curr. Opin. Drug Discov. Devel. 12(5), 616-627 (2009).
4. PAD4 is essential for antibacterial innate immunity mediated by neutrophil extracellular traps. J. Exp. Med. 207(9), 1853-1862 (2010).
5. NETosis proceeds by cytoskeleton and endomembrane disassembly and PAD4-
6. Deciphering the pathogenicity of PADI4 missense variant L117M in rheumatoid arthritis: An integrated in silico and gene expression study. Int. J. Biol. Macromol. 319(Pt 3), 145466 (2025).
7. Polymorphic analysis of genes PADI4 (rs2240340, rs1748033) and HLA-
8. Implications of peptidyl arginine deiminase 4 gene transcription and polymorphisms in susceptibility to rheumatoid arthritis in an Iranian population. BMC Med. Genomics 16(1), 104 (2023).