PAD1 Monoclonal Antibody (Clone 6B4)

Peptidyl arginine deiminase 1 (PAD1) is a calcium-dependent enzyme that catalyzes the conversion of arginine residues to citrulline within its cellular protein substrates, resulting in the loss of a positive charge, which can alter protein structure and/or function.{45610,64948} It exists as a monomer and is composed of a C-terminal catalytic domain and two N-terminal immunoglobulin-like (Ig-like) domains.{64948} PAD1 is primarily expressed in uterine and epidermal cells and generally localized in the cytosol.{19490} PAD1 citrullinates non-histone proteins, such as keratin, filaggrin, and MEK1, as well as histone H3 at arginine 2 (H3R2), H3R8, H3R17, and H4R3, to regulate epidermal cell progression and embryonic development.{64949,64950,59195} The catalytic activity of PAD1 is lost by deleting the first six N-terminal amino acids.{64948} Decreased Padi1 expression or Pad1 inhibition reduces citrullination of H3R2, H3R8, H3R17, and H4R3 and inhibits primary mouse embryo preimplantation development.{59145} PADI1 mRNA is overexpressed in tumor tissue from patients with triple-negative breast cancer (TNBC), and PAD1 promotes proliferation and epithelial-to-mesenchymal transition (EMT) in a variety of TNBC cell lines in vitro and in mouse xenograft models.{64951} Cayman's PAD1 Monoclonal Antibody (Clone 6B4) can be used for ELISA and Western blot (WB) applications. The antibody recognizes PAD1 at approximately 74 kDa from human samples.