Recombinant human NNMT protein (Active) is a Human Full Length protein, in the 1 to 264 aa range, expressed in Barley, with >95% purity and suitable for SDS-PAGE, FuncS.
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Application | Reactivity | Dilution info | Notes |
---|---|---|---|
Application SDS-PAGE | Reactivity Reacts | Dilution info - | Notes - |
Application FuncS | Reactivity Reacts | Dilution info - | Notes - |
Catalyzes the N-methylation of nicotinamide using the universal methyl donor S-adenosyl-L-methionine to form N1-methylnicotinamide and S-adenosyl-L-homocysteine, a predominant nicotinamide/vitamin B3 clearance pathway (PubMed:21823666, PubMed:23455543, PubMed:8182091). Plays a central role in regulating cellular methylation potential, by consuming S-adenosyl-L-methionine and limiting its availability for other methyltransferases. Actively mediates genome-wide epigenetic and transcriptional changes through hypomethylation of repressive chromatin marks, such as H3K27me3 (PubMed:23455543, PubMed:26571212, PubMed:31043742). In a developmental context, contributes to low levels of the repressive histone marks that characterize pluripotent embryonic stem cell pre-implantation state (PubMed:26571212). Acts as a metabolic regulator primarily on white adipose tissue energy expenditure as well as hepatic gluconeogenesis and cholesterol biosynthesis. In white adipocytes, regulates polyamine flux by consuming S-adenosyl-L-methionine which provides for propylamine group in polyamine biosynthesis, whereas by consuming nicotinamide controls NAD(+) levels through the salvage pathway (By similarity). Via its product N1-methylnicotinamide regulates protein acetylation in hepatocytes, by repressing the ubiquitination and increasing the stability of SIRT1 deacetylase (By similarity). Can also N-methylate other pyridines structurally related to nicotinamide and play a role in xenobiotic detoxification (PubMed:30044909).
Nicotinamide N-methyltransferase, NNMT
Recombinant human NNMT protein (Active) is a Human Full Length protein, in the 1 to 264 aa range, expressed in Barley, with >95% purity and suitable for SDS-PAGE, FuncS.
pH: 7.5
Constituents: 25% Glycerol (glycerin, glycerine), 0.87% Sodium chloride, 0.79% Tris HCl, 0.31% Glutathione, 0.004% (R*,R*)-1,4-Dimercaptobutan-2,3-diol, 0.003% EDTA, 0.002% PMSF
Catalyzes the N-methylation of nicotinamide using the universal methyl donor S-adenosyl-L-methionine to form N1-methylnicotinamide and S-adenosyl-L-homocysteine, a predominant nicotinamide/vitamin B3 clearance pathway (PubMed:21823666, PubMed:23455543, PubMed:8182091). Plays a central role in regulating cellular methylation potential, by consuming S-adenosyl-L-methionine and limiting its availability for other methyltransferases. Actively mediates genome-wide epigenetic and transcriptional changes through hypomethylation of repressive chromatin marks, such as H3K27me3 (PubMed:23455543, PubMed:26571212, PubMed:31043742). In a developmental context, contributes to low levels of the repressive histone marks that characterize pluripotent embryonic stem cell pre-implantation state (PubMed:26571212). Acts as a metabolic regulator primarily on white adipose tissue energy expenditure as well as hepatic gluconeogenesis and cholesterol biosynthesis. In white adipocytes, regulates polyamine flux by consuming S-adenosyl-L-methionine which provides for propylamine group in polyamine biosynthesis, whereas by consuming nicotinamide controls NAD(+) levels through the salvage pathway (By similarity). Via its product N1-methylnicotinamide regulates protein acetylation in hepatocytes, by repressing the ubiquitination and increasing the stability of SIRT1 deacetylase (By similarity). Can also N-methylate other pyridines structurally related to nicotinamide and play a role in xenobiotic detoxification (PubMed:30044909).
Belongs to the class I-like SAM-binding methyltransferase superfamily. NNMT/PNMT/TEMT family.
Deiminated by PADI1 and PADI2.
This product is an active protein and may elicit a biological response in vivo, handle with caution.
The NNMT protein also known as Nicotinamide N-methyltransferase acts by catalyzing the methylation of nicotinamide using S-adenosylmethionine as a methyl donor. This enzyme has a mass of around 29 kDa and is expressed in various tissues including liver adipose tissue and certain cancer cells. The NNMT gene provides instructions for creating the protein that plays significant roles in metabolic processes and cellular homeostasis.
NNMT impacts cell energy balance and gene expression regulation by influencing the levels of nicotinamide and methionine metabolites. This enzyme does not typically form part of a complex acting more so as an individual regulator of methylation reactions affecting cellular metabolism. Researchers find interest in NNMT for its role in modulating cellular growth and proliferation forming a link to both normal cellular functions and pathological conditions like cancer.
NNMT has a significance in NAD+ metabolism and methionine salvage pathways. These pathways are essential in maintaining redox homeostasis and proper methylation status in cells. NNMT through its enzymatic activity interacts with SAM (S-adenosyl methionine) closely relating its function to methylation processes that involve other proteins such as SIRTs (Sirtuins) and NAMPT (Nicotinamide phosphoribosyltransferase) within these metabolic pathways.
NNMT shows relevance in cancer and obesity-related complications. The protein's upregulation in cancer types like breast and colorectal cancers links it to tumor development and progression. In obesity NNMT's involvement in adipose tissue might contribute to metabolic dysregulation. The enzyme also interconnects with proteins like insulin receptors and adiponectin highlighting its potential role in metabolic diseases and making it an interesting target for therapeutic interventions.
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The specific activity of ab268816 was 220 nmol/min/mg in a methyltransferase assay using nicotinamide as substrate.
SDS-PAGE analysis of ab268816.
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