Cayman Pad4 (Human, Recombinant; Mammalian Expressed); Qty- 50; S

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 Neutrophils isolated from Pad4^-/- mice exhibit decreased citrullination of histone H3 under both basal and LPS-stimulated conditions and are defective for NET formation in response to stimulation with LPS, phorbol 12-myristate 13-acetate (PMA; Item No. 10008014), or hydrogen peroxide.⁴ Pad4^-/- mice exhibit larger lesions than wild-type mice in a model of necrotizing fasciitis induced by M1 group A S. pyogenes lacking the extracellular DNase Sda1. Pad4-deficient mice also exhibit reduced infarct size in a model of myocardial ischemia-reperfusion injury and reduced tumor growth in a Lewis lung carcinoma model.^6,2 PADI4 SNPs, including G55S, V82A, and G112A, are associated with rheumatoid arthritis in humans.⁷ Cayman’s PAD4 (human, recombinant; mammalian expressed) protein contains the G55S, V82A, and G112A SNPs and can be used for ELISA, enzyme activity assay, and Western blot (WB) applications.

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