Formulation: 50 mM Hepes, pH 8.0, with 500 mM NaCl and 10% glycerol
Purity: ≥70% estimated by SDS-PAGE
Shelf life (days): 730
Notes: S-Catechol-O-methyltransferase (S-COMT) is the soluble cytosolic form of COMT.{26887} A rough endoplasmic reticulum membrane-bound form of COMT (MB-COMT) is also encoded by the COMT gene but produced via a separate promoter and contains an additional 50 amino acid residues, which compose the membrane anchor region.{26887,26884} COMT is comprised of one domain with eight α helices surrounding a central β sheet.{55023} It is the methyltransferase responsible for transferring a methyl group from S-adenosyl-L-methionine (SAM) to a catechol hydroxyl in the inactivation or degradation of catechol-containing molecules such as catecholamines.{26885} S-COMT is involved primarily in the inactivation of endogenous and xenobiotic catechols, such as catechol-containing hormones and carcinogenic flavonoids, and MB-COMT is involved primarily in the degradation of endogenous catecholamine neurotransmitters.{26885,26888} S-COMT is the predominant form of COMT and is found primarily in the liver and kidney but is also found in the stomach, small intestine, adrenal gland, spleen, and brain.{55021} A valine-to-methionine substitution (Val158Met) in COMT affects its thermostability and may reduce its activity by greater than 50% in the human brain.{26886} The Val158Met variant of COMT is associated with Parkinson’s disease in an ethnicity-dependent manner.{55022} COMT interacts with severe acute respiratory coronavirus 2 (SARS-CoV-2) non-structural protein 7 (Nsp7), which, together with Nsp8, forms the primase complex of the replicase-transcriptase complex of SARS-CoV-2.{55024} Cayman’s S-Catechol-O-Methyltransferase (human, recombinant) protein can be used for ELISA, Western blot (WB), and enzyme activity assay applications.
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