Post-translational modification of histones plays a crucial role in DNA transcription, chromatin function and overall maintenance of cell signaling pathways. Citrullination is one of the many crucial histone modifications catalyzed by a family of enzymes called Protein Arginine Deiminases (PADs). PADs catalyze the hydrolysis of peptidyl-arginine to form peptidyl-citrulline on histone proteins regulating many biochemical processes related to the chromatin architecture (1).
PAD family consists of five members of calcium-dependent isozymes PAD1, 2, 3, 4, and 6. Histone citrullination impacts chromatic structure by converting arginine amino acid on histones leading to the reduction in hydrogen bonding and decondensation of the chromatin structure. Notable studies have established PADs as an important target for drug discovery projects related to many human diseases such as cancer, autoimmune diseases (rheumatoid arthritis), and inflammatory diseases.
SignalChem’s scientists have developed a full range of five mammalian PADs and PAD assay cocktails with superior quality to facilitate your drug discovery and development activities. Our recombinant PADs (PAD1, PAD4, PAD3, PAD6, and PAD2) and their assay cocktails are the effective in vitro tools to investigate protein citrullination in various human diseases.
(1). Bicker, K. L., & Thompson, P. R. (2013). The protein arginine deiminases (PADs): Structure, Function, Inhibition, and Disease. Biopolymers, 99(2), 155–163. http://doi.org/10.1002/bip.22127