Human/Primate Dopamine beta-Hydroxylase N-Terminus Antibody

Dopamine beta-hydroxylase (D betaH; also dopamine beta-monooxygenase) is a 73-77 kDa member of the copper type II ascorbate-dependent monooxygenase family. It is both soluble (73 kDa) and membrane-bound (77 kDa) (anchored by an uncleaved signal sequence), and via hydroxylation, converts dopamine into norepinepherine. Human D betaH is a copper-containing disulfide-linked homodimer that is found in neurons and adrenal medullary cells. It is 603 amino acids (aa) in length and contains a 25 aa signal sequence followed by three domains. The first is an N-terminal 120 aa DOMON domain (dopamine beta-monooxygenase N-terminal) that may either bind D betaH to the cell membrane, or participate in tetramerization. This is followed by two 150 aa Cu⁺-type II ascorbate-dependent monooxygenase domains (aa 182-330 and 352-512). D betaH may be most active as a dimeric-dimer/tetramer, whose association status is dependent on local Cl^- concentrations.