epitope mapping within an internal region of OAT of human origin
recommended for detection of hepatic and renal forms of ornithine aminotransferase of mouse, rat and human origin by ELISA; also reactive with additional species, including equine, canine, bovine, porcine and avian
OAT Background Information OAT (ornithine aminotransferase (mitochondrial), ornithine-oxo-acid aminotransferase) is a 439 amino acid protein encoded by the human gene OAT. OAT belongs to the class III pyridoxal-phosphate-dependent aminotransferase family and is usually found as a homotetramer in the mitochondrion matrix. OAT catalyzes the major catalytic reaction for ornithine. Ornithinemia, presumably due to deficiency of ornithine ketoacid aminotransferase (OAT) has been found in patients with gyrate atrophy of the choroid and retina. The clinical history of gyrate atrophy is usually night blindness that begins in late childhood, accompanied by sharply demarcated circular areas of chorioretinal atrophy. During the second and third decades the areas of atrophy enlarge. The hepatic cleavage product, hepatic OAT, is formed by cleaving a 25 amino acid transit peptide from the N-terminus of the OAT precursor. The renal form is produced by cleaving a 35 amino acid transit peptide from the N-terminus.
