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Recombinant Human COMT Protein, CF

R&D Systems, part of Bio-Techne | Catalog # 7386-MT

R&D Systems, part of Bio-Techne
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7386-MT-010

Key Product Details

Source

E. coli

Accession #

Conjugate

Unconjugated

Applications

Enzyme Activity

Product Specifications

Source

E. coli-derived human COMT protein
Gly52-Pro271, with an N-terminal Met and a C-terminal 6-His tag

Purity

>90%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining.

Endotoxin Level

<0.10 EU per 1 μg of the protein by the LAL method.

N-terminal Sequence Analysis

Gly52

Predicted Molecular Mass

25 kDa

SDS-PAGE

24-26 kDa, reducing conditions

Activity

Measured by its ability to methylate catechol to O-methyl-catechol.
The specific activity is >95 pmol/min/μg, as measured under the described conditions.

Formulation, Preparation and Storage

7386-MT
Formulation Supplied as a 0.2 μm filtered solution in Tris, NaCl, Glycerol and TCEP.
Shipping The product is shipped with polar packs. Upon receipt, store it immediately at the temperature recommended below.
Stability & Storage Use a manual defrost freezer and avoid repeated freeze-thaw cycles.
  • 6 months from date of receipt, -20 to -70 °C as supplied.
  • 3 months, -20 to -70 °C under sterile conditions after opening.

Background: COMT

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).

References

  1. Zhu, B. T. (2002) Curr. Drug Metab. 3:321.

  2. Lotta, T. et al. (1995) Biochemistry 34:4202.

  3. Lachman. H. M. et al. (1996) Pharmacogenetics 6:243.

  4. Rutherford, K. et al. (2008) Biochim. Biophys. Acta 1784:1098.

  5. Dickinson, D. and Elvevag, B. (2009) Neuroscience 164:72.

Long Name

Catechol O-Methyltransferase

Alternate Names

catechol O-methyltransferase, catechol-O-methyltransferase, EC 2.1.1.6

Entrez Gene IDs

1312 (Human)

Gene Symbol

COMT

UniProt

Additional COMT Products

Product Documents for Recombinant Human COMT Protein, CF

Certificate of Analysis

To download a Certificate of Analysis, please enter a lot number in the search box below.

Note: Certificate of Analysis not available for kit components.

Product Specific Notices for Recombinant Human COMT Protein, CF

For research use only

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