Cayman PAD2 (human, recombinant)

Peptidyl arginine deiminase 2 (PAD2) catalyzes the conversion of arginine residues to citrulline within cellular protein substrates, resulting in the loss of a positive charge, which can alter protein structure and/or function. It is composed of an α/β propeller domain, an IgG1 domain that contains calcium binding sites, and an IgG2 domain. PAD2 changes conformation upon calcium binding to the IgG1 domain, which activates PAD2 and allows its substrates to bind. It is ubiquitously expressed with high expression in the brain, spleen, muscle, and spinal cord and is localized primarily to the cytoplasm but can translocate to the nucleus in response to calcium signaling.^,,, PAD2 citrullinates non-histone proteins, such as glial fibrillary acid protein (GFAP), myelin basic protein (MBP), and retinoic acid receptor-related orphan receptor γ (RORγ), as well as histone H3 at arginine 26 (H3R26), to regulate diverse processes ranging from myelination to immune function. PADI2, the gene encoding PAD2, is highly expressed in tumors from patients with breast cancer and associated with poor prognosis. It is also overexpressed in a variety of other cancers, including castration-resistant prostate, ovarian, and lung cancers, among others. PAD2 has been found in the synovial fluid of patients with rheumatoid arthritis (RA), and anti-PAD2 antibodies are associated with less severe RA than patients with autoantibodies to PAD4. Cayman’s PAD2 (human recombinant) protein can be used for enzyme activity assays.

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