COMT Protein, Human (sf9, His)

Catechol-O-methyltransferase (COMT) plays a crucial role by catalyzing and inactivating the O-methylation of catecholamine neurotransmitters and catechol hormones. This enzyme activity is critical for regulating the biological half-life of key neuroactive compounds, including catecholamines. COMT Protein, Human (sf9, His) is the recombinant human-derived COMT protein, expressed by Sf9 insect cells , with C-His labeled tag. The total length of COMT Protein, Human (sf9, His) is 221 a.a., with molecular weight of ~20.3 kDa.

Catechol-O-methyltransferase (COMT) is a crucial enzyme that catalyzes the O-methylation and subsequent inactivation of catecholamine neurotransmitters and catechol hormones. By mediating the transfer of a methyl group to these molecules, COMT plays a pivotal role in regulating the levels and activity of neurotransmitters such as dopamine, epinephrine, and norepinephrine. Beyond its involvement in catecholamine metabolism, COMT also shortens the biological half-lives of specific neuroactive drugs, including L-DOPA, alpha-methyl DOPA, and isoproterenol. This enzymatic activity is significant in modulating the pharmacokinetics of therapeutic agents targeting neurological and hormonal pathways. The regulatory role of COMT in both endogenous neurotransmitters and exogenous drugs highlights its importance in the fine-tuning of neurotransmission and drug responses, showcasing its broad impact on physiological and pharmacological processes.

Human

Sf9 insect cells

C-His

P21964 (M51-P271)

1312  [NCBI]

Approximately 20.3 kDa

Greater than 90% as determined by reducing SDS-PAGE.

<1 EU/μg, determined by LAL method.