Analytical Data
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Gene name
Carnmt1
- Application
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Species
Mouse
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Source
E. coli
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Tag
N- His-SUMO
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
Q80UY1
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Expression Region
50-400aa
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Molecular Weight
54.2 kDa
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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
Carnitine acetyltransferase (Carnmt1) has garnered significant attention in recent years due to its crucial role in metabolic pathways, particularly in the regulation of fatty acid metabolism and energy homeostasis. This enzyme facilitates the transfer of an acetyl group from acetyl-CoA to carnitine, forming acetylcarnitine, which is essential for the transport of fatty acids into mitochondria, where they undergo β-oxidation to generate ATP. Dysregulation of Carnmt1 activity has been linked to various metabolic disorders, including obesity, diabetes, and cardiovascular diseases. Research into the characterization of recombinant Carnmt1 protein has advanced our understanding of its structure-function relationships, substrate specificity, and kinetic parameters, providing valuable insights for potential therapeutic applications. Additionally, the development of Carnmt1 inhibitors or enhancers could pave the way for novel interventions in metabolic diseases by modulating fatty acid oxidation and overall energy metabolism. As such, investigating the recombinant protein of Carnmt1 not only contributes to the fundamental knowledge of metabolic biochemistry but also holds promise for clinical implications in managing metabolic health.
