ADAR2 (F6U8S) Rabbit Monoclonal Antibody recognizes endogenous levels of total ADAR2 protein. This antibody detects a non-specific band of unknown origin at 180 kDa that might represent the ADAR2 homodimer.

Monoclonal antibody is produced by immunizing animals with a synthetic peptide corresponding to residues near the carboxy terminus of human ADAR2 protein.

ADAR2, also known as RED1, is an enzyme that catalyzes the adenosine (A) to inosine (I) editing of double-stranded RNA (dsRNA) (1). This is the most common type of RNA editing in mammals, and because inosine is read as guanosine by the cellular machinery, ADAR2 can effectively alter genetic information at the RNA level (2,3). ADAR2 is known to be efficient and perform site-specific editing, thereby modulating encoded protein properties (4). ADAR2 can influence RNA stability by modifying the access of RNA-binding proteins, particularly decay-promoting factors (5), and has also been shown to affect alternative splicing (6). Importantly, ADAR2 forms a homodimer complex, which is critical for its functions (7,8). Dysregulation of ADAR2 activity has been implicated in various human diseases, including amyotrophic lateral sclerosis (ALS), where reduced ADAR2-mediated editing of GluA2, a subunit of the L-α-amino-3-hydroxy-5-methyl-4-isoxazolepropionic acid (AMPA) receptor, has been observed (9). ADAR2 has also been linked to cancer, with altered ADAR2 expression correlating with malignancy in different tumor types. ADAR2 also edits numerous miRNAs and contributes to tumorigenesis regulation by balancing the functions of oncogenic and tumor-suppressive miRNAs (10,11). ADAR2 can also display tumor-suppressive functions. For example, ADAR2 is downregulated in approximately 50% of hepatocellular carcinoma (HCC), and overexpression of ADAR2 in ADAR-deficient HCC cells reduces their oncogenic potential (12).