Analytical Data
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Gene name
NNMT
- 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 90% as determined by SDS-PAGE.
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Uniprot
O55239
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Expression Region
Met1~Glu264
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Molecular Weight
27kDa
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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
NNMT (Nicotinamide N-methyltransferase) is an important enzyme that plays a crucial role in the methylation of nicotinamide, influencing various metabolic pathways and cellular functions. Research on NNMT has gained significant attention due to its implications in several physiological processes and its potential link to various diseases, including metabolic disorders, cancer, and neurodegenerative conditions. Elevated NNMT levels have been associated with obesity and insulin resistance, highlighting its potential as a therapeutic target for metabolic diseases. Furthermore, NNMT is involved in the regulation of the NAD+ (nicotinamide adenine dinucleotide) metabolism, which is essential for cellular energy production and mitochondrial function. Understanding the structural and functional characteristics of NNMT through recombinant protein studies can provide insights into its enzymatic mechanisms and regulatory roles. The development of recombinant NNMT proteins allows for detailed investigations into substrate specificity, enzyme inhibition, and the effects of genetic variations on enzyme activity. This knowledge is essential for the development of potential inhibitors or modulators that can be used in clinical settings to manage related diseases. Overall, the study of NNMT and its recombinant proteins serves as a promising avenue for advancing our understanding of metabolic regulation and discovering novel therapeutic strategies.
