Human Dopamine beta-Hydroxylase Alexa Fluor® 647-conjugated Antibody

Applications

Please Note: Optimal dilutions should be determined by each laboratory for each application. General Protocols are available in the Technical Information section on our website.

Preparation and Storage

Background: Dopamine beta-Hydroxylase

DBH (Dopamine beta -Hydroxylase) is a 77-78 kDa member of the Cu⁺⁺ type II ascorbate-dependent monooxygenase family of enzymes. It is expressed in noradrenergic nerve terminals and adrenal medullary chromaffin cells, and serves as a catalyst for the conversion of dopamine into norepinepherine. Unlike its family member counterparts (TH and PNMT) that are cytosolic, DBH is embedded in the membranes of secretory vesicles. Human DBH is a 617 amino acid (aa) type II transmembrane glycoprotein (SwissProt # P09172). It contains an N-terminal 16 aa cytoplasmic region, plus a 580 aa lumenal domain (aa 38-617). The luminal region possesses one DOMON (dopamine beta -monooxygenase N-terminal) domain (aa 51-169) plus two consecutive monooxygenase motifs (aa 214-523). DBH exists as both a membrane-embedded 77-78 kDa isoform, and a soluble 73-75 kDa isoform. The latter may arise from cleavage following Gly39. Structurally, DBH will form a disulfide-linked homodimer, which then noncovalently associates with another DBH covalent homodimer, generating a functional 290 kDa homotetramer. Over aa 37‑617, human DBH shares 79% aa sequence identity with mouse DBH.

Product Datasheets

Related Research Areas

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• Oxygenases/Hydroxylases
• Parkinson's Disease Related Molecules
• Redox Enzymes