Analytical Data
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Gene name
COMT
- Application
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Species
Mouse
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Source
E. coli
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Tag
N-His
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Purity
Greater than 95% as determined by SDS-PAGE.
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Uniprot
O88587
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Expression Region
Arg20~Ser265
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Molecular Weight
29kDa
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Endotoxin
< 1.0 EU per μg protein as determined by the LAL method.
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Form
Freeze-dried powder
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Buffer formulation
PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300.
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Reconstitution
Reconstitute in ddH2O to a concentration of 0.1-0.5 mg/mL. Do not vortex.
- Customization
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Stability Test
The thermal stability is described by the loss rate. The loss rate was determined by accelerated thermal degradation test, that is, incubate the protein at 37℃ for 48h, and no obvious degradation and precipitation were observed. The loss rate isless than 8% within the expiration date under appropriate storage condition.
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Storage & Shelf Life
Samples are stable for up to twelve months from date of receipt at -20℃ to -80℃. Store it under sterile conditions at -20℃ to -80℃. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.
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Shipping
In general, recombinant proteins are supplied as lyophilized powder and shipped at ambient temperature. For bulk packages, the proteins are provided as frozen liquid and shipped with blue ice, unless otherwise requested by the customer.
Quality inspection process
Related Products
Protein Description
Catechol-O-methyltransferase (COMT) is a pivotal enzyme involved in the metabolism of catecholamines, such as dopamine, epinephrine, and norepinephrine. Its role is crucial in regulating neurotransmitter levels, thus influencing various physiological and psychological processes, including mood, cognition, and stress response. COMT operates through the transfer of a methyl group from S-adenosylmethionine (SAM) to catechol compounds, rendering them less active and promoting their excretion. Genetic variations, particularly the COMT Val158Met polymorphism, have been linked to differential enzyme activity, impacting individual susceptibility to neuropsychiatric disorders, such as schizophrenia and depression. The study of recombinant COMT proteins has gained momentum in recent years, enabling researchers to investigate the structure-function relationships of the enzyme in detail, assess the effects of genetic variants, and discover potential therapeutic targets. By producing and characterizing recombinant forms of the enzyme, researchers can enhance our understanding of its catalytic mechanisms, develop inhibitors, and explore its role in various signaling pathways. Furthermore, recombinant COMT proteins provide valuable tools for studying the interaction of the enzyme with other proteins and small molecules, paving the way for innovative therapeutic strategies aimed at modulating catecholamine pathways in the treatment of mental health disorders. Overall, the exploration of COMT as a recombinant protein serves not only to elucidate its biochemical properties but also to advance our understanding of the neurobiological underpinnings of a range of psychiatric conditions.
