PADI2 (E3P8Z) Rabbit mAb #97647

Peptidyl arginine deiminase (PAD) proteins are a family of Ca²⁺-dependent enzymes that catalyze the post-translational conversion of arginine to citrulline. There are currently five known PAD isozymes in humans, referred to as PADI1-4 and PADI6 (1). Among these isozymes, peptidyl arginine deiminase type 2 (PADI2) is the most widely expressed, being found in skeletal muscle, brain, colon, breast, macrophages, spleen, and spinal cord tissue, among others (1,2). In normal mouse development, PADI2 expression levels are elevated from 18 days to 2 months of age, and gradually decrease from 3 months onward (3). Some of the most well studied PADI2 substrates include vimentin, actin, myelin basic protein (MBP), glial fibrillary acidic protein (GFAP), and histones (4). PADI2-mediated citrullination has been shown to be involved in neurodegeneration and inflammatory response-associated diseases such as multiple sclerosis (MS), Alzheimer’s disease (AD), psoriasis, and rheumatoid arthritis (5). Excessive PAD-mediated deimination of MBP is believed to be a major contributor to MS disease progression, while elevated levels of citrullinated GFAP and vimentin proteins have been found in the brains of AD patients (2,4). PADI2 has also been found to play a role in the progression of several types of cancers, including colorectal, breast, and prostate (5-7).