PAD3 (human, recombinant)

Protein arginine deiminase 3 (PAD3) catalyzes the conversion of arginine residues to citrulline within its cellular protein substrates, which include S100A3, trichohyalin, and filaggrin, resulting in the loss of a positive charge, which can alter protein structure and/or function.¹ It exists as a homodimer and is composed of a C-terminal catalytic domain and an N-terminal domain that contains two immunoglobulin G (IgG) subdomains.² PAD3 is primarily expressed by differentiated keratinocytes in the epidermis and hair follicles where it has roles in the shaping and mechanical strengthening of hair.^2,3 It is also expressed by neural stem cells where it modulates cell death by regulating the nuclear translocation of apoptosis-inducing factor (AIF), in mammary glands where it citrullinates proteins during lactation, and cancer cells where it promotes cancer cell invasion.^4,5,6 Mutations in PADI3 are associated with uncombable hair syndrome. Cayman's PAD3 (human, recombinant) protein can be used for enzyme activity assays.

WARNING This product is not for human or veterinary use.

1. van Beers, J.J.B.C., Zendman, A.J.W., Raijmakers, R., et al. Peptidylarginine deiminase expression and activity in PAD2 knock-out and PAD4-low mice. Biochimie 95(2), 299-308 (2013).

2. Funabashi, K., Sawata, M., Nagai, A., et al. Structures of human peptidylarginine deiminase type III provide insights into substrate recognition and inhibitor design. Arch. Biochem. Biophys. 708, 108911 (2021).

3. Basmanav, F.B.Ü., Cau, L., Tafazzoli, A., et al. Mutations in three genes encoding proteins involved in hair shaft formation cause uncombable hair syndrome. Am. J. Cancer Res. 99(6), 1292-1304 (2016).

4. U, K.P., Subramanian, V., Nicholas, A.P., et al. Modulation of calcium-induced cell death in human neural stem cells by the novel peptidylarginine deiminase-AIF pathway. Biochim. Biophys. Acta 1843(6), 1162-1171 (2014).

5. Li, G., Hayward, I.N., Jenkins, B.R., et al. Peptidylarginine deiminase 3 (PAD3) is upregulated by prolactin stimulation of CID-9 cells and expressed in the lactating mouse mammary gland. PLoS One 11(1), e0147503 (2016).

6. Uysal-Onganer, P., D'Alessio, S., Mortoglou, M., et al. Peptidylarginine deiminase inhibitor application, using Cl-amidine, PAD2, PAD3 and PAD4 isozyme-specific inhibitors in pancreatic cancer cells, reveals roles for PAD2 and PAD3 in cancer invasion and modulation of extracellular vesicle signatures. Int. J. Mol. Sci. 22(3), 1396 (2021).

Gorzeń, O., Mikołajczyk-Martinez, A., Mamun, A.A., et al. Isoform-selective PAD2/PAD4 substrates with unnatural amino acids enable cellular peptidylarginine deiminase activity profiling and reveal vimentin citrullination effects in macrophages. Biochemistry 64(19), 4105-4120 (2025).

Yao, H., Cao, G., Liu, Z., et al. Inhibition of netosis with PAD inhibitor attenuates endotoxin shock induced systemic inflammation. Int. J. Mol. Sci. 23(21), 13264 (2022).