Catechol-O-methyltransferase (COMT) catalyzes the transfer of the methyl group from S- adenosyl-L-methionine to either the meta- or the para-hydroxyl group of the catechol ring from a variety of endogenous and exogenous catechol substrates including the neurotransmitters dopamine, epinephrine, and norepinephrine (1). Thus, it plays important roles in one of the major degradative pathways of the catecholamine transmitters, and in the metabolism of catechol drugs used in the treatment of hypertension, asthma, and Parkinson’s disease. In tissues, COMT is produced as two distinct forms, a soluble protein (residues 52-271) and a membrane-bound protein that possesses the N-terminal transmembrane domain (2). A common single-nucleotide polymorphism results in substitution of methionine for valine at position 158 of membrane-bound COMT and position 108 at soluble COMT (3). This amino acid change results in a more unstable and three- to four -fold less active 108/158Met form (4). Since COMT activity is the major regulator of dopamine function in the prefrontal brain region, the Val108/158Met variation is considered to be associated with increased risk of a wide spectrum of mental disorders (5).||Source:|Recombinant protein corresponding to human COMT, fused to his-tag at C-terminal, expressed in E. coli.||Molecular Weight: |~25kD||Endotoxin:|<0.10EU/1ug (LAL method).||Storage and Stability:|May be stored at 4°C for short-term only. Aliquot to avoid repeated freezing and thawing. Store at -20°C. For maximum recovery of product, centrifuge the original vial after thawing and prior to removing the cap. Further dilutions can be made in assay buffer.

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