PADI2
PADI2 (peptidyl arginine deiminase 2, also known as PDI2 or KIAA0994) is a cytoplasmic enzyme that catalyses the deimination of arginine residues in proteins. It belongs to the protein arginine deiminase family and is the most widely expressed of its members. Browse Assay Genie's current range of PADI2 research reagents below, or read on for the biology behind the target.
PADI2 catalyses the post-translational deimination of proteins, converting arginine residues into citrullines in the presence of calcium ions. This modification, known as citrullination, alters the protein substrate after it has been synthesised. UniProt describes the enzyme's function as the deimination of arginine residues of proteins, and it is assigned EC 3.5.3.15.
The PADI2 gene encodes a member of the peptidyl arginine deiminase family, whose members have distinct substrate specificities and tissue-specific expression patterns. The type II enzyme is the most widely expressed family member. Known substrates include myelin basic protein in the central nervous system and vimentin in skeletal muscle and macrophages. The protein is found in the cytoplasm. Researchers studying the PADI2 protein often compare it with other family members such as PADI4 and PADI6.
The enzyme is thought to play a role in the onset and progression of neurodegenerative human disorders, including Alzheimer disease and multiple sclerosis, and it has also been implicated in glaucoma pathogenesis. The PADI2 gene sits in a cluster with four other paralogous genes. It was previously named peptidyl arginine deiminase, type II, and the HGNC groups it under the peptidyl arginine deiminases. Mouse and rat both have a Padi2 ortholog, which supports comparative work in model systems.
PADI2 converts peptidyl arginine to citrulline in a calcium-dependent reaction, making it a central enzyme for studying this post-translational modification.
PADI2 is thought to contribute to the onset and progression of Alzheimer disease and multiple sclerosis, and it deiminates myelin basic protein in the central nervous system.
PADI2 has been implicated in glaucoma pathogenesis, which makes it a candidate for studies of deimination in disease mechanisms.
Vimentin is a known PADI2 substrate in skeletal muscle and macrophages, so the enzyme is relevant to work on these tissues.
PADI2 catalyses the deimination of arginine residues in proteins, converting them into citrullines in the presence of calcium ions. Known substrates include myelin basic protein in the central nervous system and vimentin in skeletal muscle and macrophages.
PADI2 is the HGNC symbol for peptidyl arginine deiminase 2. Aliases include PDI2 and KIAA0994, and the earlier name was peptidyl arginine deiminase, type II. UniProt lists the protein as protein-arginine deiminase type-2.
PADI2 is thought to play a role in neurodegenerative disorders, including Alzheimer disease and multiple sclerosis, and has been implicated in glaucoma. Mouse and rat each have a Padi2 ortholog. Check the datasheet of any product for its validated reactivity.
Other peptidyl arginine deiminase family members that catalyse protein citrullination.
Gene and protein annotations from HGNC, NCBI Gene and UniProt Q9Y2J8; product specifications from Assay Genie datasheets.