protein

Nicotinamide N-Methyltransferase/NNMT Protein, Human (His)

HY-P79286

50 μg;100 μg

280;475 USD

Nicotinamide N-Methyltransferase/NNMT Protein, Human (His)

proteins

E. coli

50 μg;100 μg

280;475 USD

The nicotinamide N-methyltransferase (NNMT) protein catalyzes the methylation of nicotinamide using S-adenosyl-L-methionine to form N1-methylnicotinamide. NNMT affects pluripotent embryonic stem cell development and acts as a metabolic regulator, affecting adipose tissue energy expenditure, gluconeogenesis, and cholesterol biosynthesis. Nicotinamide N-Methyltransferase/NNMT Protein, Human (His) is the recombinant human-derived Nicotinamide N-Methyltransferase/NNMT protein, expressed by E. coli , with C-His labeled tag. The total length of Nicotinamide N-Methyltransferase/NNMT Protein, Human (His) is 264 a.a., with molecular weight of ~25-30 kDa.

Human

Nicotinamide N-Methyltransferase (NNMT) is responsible for catalyzing the N-methylation of nicotinamide, utilizing the universal methyl donor S-adenosyl-L-methionine to produce N1-methylnicotinamide and S-adenosyl-L-homocysteine, representing a prominent pathway for nicotinamide/vitamin B3 clearance. This enzymatic activity plays a central role in cellular methylation potential regulation by consuming S-adenosyl-L-methionine, thus limiting its availability for other methyltransferases. NNMT actively orchestrates genome-wide epigenetic and transcriptional changes through the hypomethylation of repressive chromatin marks, such as H3K27me3, and contributes to the establishment of low levels of repressive histone marks in pluripotent embryonic stem cell pre-implantation state during development. Functionally, NNMT acts as a metabolic regulator impacting white adipose tissue energy expenditure, hepatic gluconeogenesis, and cholesterol biosynthesis. In white adipocytes, it regulates polyamine flux and controls NAD(+) levels through the salvage pathway. Additionally, NNMT, by producing N1-methylnicotinamide, influences protein acetylation in hepatocytes, repressing the ubiquitination and enhancing the stability of the SIRT1 deacetylase. Furthermore, NNMT exhibits versatility by N-methylating other pyridines structurally related to nicotinamide, suggesting a role in xenobiotic detoxification.

Nicotinamide N-methyltransferase; NNMT

Greater than 95% as determined by reducing SDS-PAGE

Supplied as a 0.2 μm filtered solution of 50 mM Tris-HCL, 300 mM NaCl, pH 7.4, 10% Glycerol.

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