The ADAR (adenosine deaminase that acts on RNA) enzyme, previously known as DRADA, is involved in the RNA editing of glutamate-gated ion channels and the serotonin-2C receptor. This novel enzyme is implicated in central nervous system disorders characterized by abnormal neuronal transmission and intracellular signaling in mammalian brain such as stroke, schizophrenia, depression, and substance abuse.

Adenosine Deaminase Acting on RNA (ADAR) is a member of a gene family that is involved in site-selective RNA editing that changes adenosine residues to inosine.  Three vertebrate ADAR gene family members, ADAR1, ADAR2,and ADAR3, have been identified.  ADAR1 and ADAR2 form a stable enzymatically active homodimer complex and ADAR3is a monomeric, enzymatically inactive form.

anti-ADAR1 (made against dsRNA binding domain region)

References:    Q. Wang et al.  (2000)  Requirement of the RNA Editing Deaminase ADAR1 Gene for Embryonic Erythropoiesis, Science Vol. 290, 1765-1768

                        Dan-Sung C. Cho et al. (2003)  Requirement of Dimerization for RNA Editing Activity of Adenosine Deaminases Acting on RNA, The Journal of Biological Chemistry Vol. 278 No. 19, 17093-17102

anti-ADAR2 (made against N-terminal region)

References:    Dan-Sung C. Cho et al. (2003)  Requirement of Dimerization for RNA Editing Activity of Adenosine Deaminases Acting on RNA, The Journal of Biological Chemistry Vol. 278 No. 19, 17093-17102

anti-ADAR3 (made against N-terminal region)

References:    Chun-Xia Chen et al.  (2000)  A third member of the RNA-specific adenosine deaminase gene family, ADAR3, contains both single- and double-stranded RNA binding domains, RNA Vol. 6, 755-767