NNMT Protein, Human (GST)

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. NNMT Protein, Human (GST) is the recombinant human-derived NNMT protein, expressed by E. coli , with N-GST labeled tag. The total length of NNMT Protein, Human (GST) is 264 a.a., with molecular weight of 56.6 kDa.

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.

Human

E. coli

N-GST

P40261 (M1-L264)

4837

56.6 kDa

Greater than 90 % as determined by reducing SDS-PAGE.

Lyophilized powder

Lyophilized from a 0.22 μm filtered solution of PBS, 6% Trehalose, pH 7.4.

<1 EU/μg, determined by LAL method.

It is not recommended to reconstitute to a concentration less than 100 μg/mL in ddH₂O.

Stored at -20°C for 2 years. After reconstitution, it is stable at 4°C for 1 week or -20°C for longer (with carrier protein). It is recommended to freeze aliquots at -20°C or -80°C for extended storage.

Room temperature in continental US; may vary elsewhere.