epitope mapping at the C-terminus of ADAT1 of mouse origin
recommended for detection of ADAT1 of mouse, rat and human origin by ELISA; also reactive with additional species, including equine, canine and porcine
ADAT1 Background Information Editing of RNA alters the nucleotide sequence of a transcript to produce codon changes, which can result in alternative translation patterns from a single pre-mRNA. One type of RNA editing involves tRNA-specific adenosine deaminase, ADAT1, which is responsible for the first step in the processing of eukaryotic tRNAAla transcripts that undergo specific adenosine to inosine modifications. Additionally, members of the double-stranded RNA (dsRNA) adenosine deaminase family of enzymes, ADAR1 and ADAR2, act on double-stranded regions of RNA. dsRNA structures are formed by base pairing of an exonic sequence around the editing site with a complementary sequence in the downstream intron. ADAR family member-mediated editing occurs in the nucleus before splicing removes the respective intron. These enzymes all faciliate the deamination of adenosine to generate inosine, which is then translated as guanosine. ADAR1, ADAR2 and a related brain-specific ADAR family member, RED2, contain a central series of double-stranded RNA-binding motifs and a C-terminal catalytic domain. ADAR1 also contains a novel Za-DNA binding domain at the N-terminal region, and when bound to Z-DNA-ADAR1 is substantially less susceptible to proteolytic degradation.
