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Mouse Anti-NNMT Recombinant Antibody (3D8) (CBMAB-N2846-WJ)

This product is a Mouse antibody that recognizes NNMT. The antibody 3D8 can be used for immunoassay techniques such as: WB, FC, IHC, IF, IHC-P.
See all NNMT antibodies
Published Data
Fig.1 NNMT expression in MKN28, SGC7901, MGC803, and BGC823 cell lines.
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Fig.2 NNMT was expressed in both the cytoplasm and stroma, as indicated by strong IHC staining.
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Fig.1 NNMT expression in MKN28, SGC7901, MGC803, and BGC823 cell lines.
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Fig.2 Representative presentation of NNMT protein expression in pancreatic tissues on tissue microarray sections by IHC.
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Summary

Host Animal
Mouse
Specificity
Human, Mouse
Clone
3D8
Antibody Isotype
IgG2b
Application
WB, FC, IHC, IF, IHC-P

Basic Information

Specificity
Human, Mouse
Antibody Isotype
IgG2b
Clonality
Monoclonal
Application Notes
The COA includes recommended starting dilutions, optimal dilutions should be determined by the end user.

Formulations & Storage [For reference only, actual COA shall prevail!]

Format
Liquid
Buffer
PBS, pH 7.3, 1% BSA, 50% glycerol
Preservative
0.02% sodium azide
Concentration
1 mg/mL
Storage
Store at +4°C short term (1-2 weeks). Aliquot and store at -20°C long term. Avoid repeated freeze/thaw cycles.

Target

Full Name
Nicotinamide N-Methyltransferase
Introduction
N-methylation is one method by which drug and other xenobiotic compounds are metabolized by the liver. This gene encodes the protein responsible for this enzymatic activity which uses S-adenosyl methionine as the methyl donor. [provided by RefSeq, Jul 2008]
Entrez Gene ID
Human4837
Mouse18113
UniProt ID
HumanP40261
MouseO55239
Alternative Names
Nicotinamide N-Methyltransferase; EC 2.1.1.1;
Function
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:8182091. PubMed:21823666, PubMed:23455543).
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:26571212, PubMed:23455543, 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).
Biological Process
Animal organ regenerationIEA:Ensembl
MethylationTAS:Reactome
NAD biosynthesis via nicotinamide riboside salvage pathwayTAS:Reactome
Nicotinamide metabolic processManual Assertion Based On ExperimentIDA:UniProtKB
Positive regulation of gluconeogenesisISS:UniProtKB
Positive regulation of protein deacetylationISS:UniProtKB
Regulation of histone H3-K4 methylationIEA:Ensembl
Regulation of histone methylationManual Assertion Based On ExperimentIMP:UniProtKB
Regulation of polyamine biosynthetic processIEA:Ensembl
Response to organonitrogen compoundIEA:Ensembl
Response to xenobiotic stimulusIEA:Ensembl
Cellular Location
Cytoplasm
PTM
Deiminated by PADI1 and PADI2.

Wang, W., Yang, C., Wang, T., & Deng, H. (2022). Complex roles of nicotinamide N-methyltransferase in cancer progression. Cell Death & Disease, 13(3), 267.

Takahashi, R., Kanda, T., Komatsu, M., Itoh, T., Minakuchi, H., Urai, H., ... & Itoh, H. (2022). The significance of NAD+ metabolites and nicotinamide N-methyltransferase in chronic kidney disease. Scientific reports, 12(1), 6398.

Parsons, R. B., & Facey, P. D. (2021). Nicotinamide N-methyltransferase: an emerging protagonist in cancer macro (r) evolution. Biomolecules, 11(10), 1418.

Roberti, A., Fernández, A. F., & Fraga, M. F. (2021). Nicotinamide N-methyltransferase: At the crossroads between cellular metabolism and epigenetic regulation. Molecular Metabolism, 45, 101165.

Campagna, R., Mateuszuk, Ł., Wojnar-Lason, K., Kaczara, P., Tworzydło, A., Kij, A., ... & Chlopicki, S. (2021). Nicotinamide N-methyltransferase in endothelium protects against oxidant stress-induced endothelial injury. Biochimica et Biophysica Acta (BBA)-Molecular Cell Research, 1868(10), 119082.

Gao, Y., Martin, N. I., & van Haren, M. J. (2021). Nicotinamide N-methyl transferase (NNMT): An emerging therapeutic target. Drug Discovery Today, 26(11), 2699-2706.

Campagna, R., Pozzi, V., Sartini, D., Salvolini, E., Brisigotti, V., Molinelli, E., ... & Emanuelli, M. (2021). Beyond Nicotinamide Metabolism: Potential Role of Nicotinamide N-Methyltransferase as a Biomarker in Skin Cancers. Cancers, 13(19), 4943.

Togni, L., Mascitti, M., Sartini, D., Campagna, R., Pozzi, V., Salvolini, E., ... & Emanuelli, M. (2021). Nicotinamide N-Methyltransferase in head and neck tumors: A comprehensive review. Biomolecules, 11(11), 1594.

Ramsden, D. B., Waring, R. H., Parsons, R. B., Barlow, D. J., & Williams, A. C. (2020). Nicotinamide N-methyltransferase: genomic connection to disease. International Journal of Tryptophan Research, 13, 1178646920919770.

Gao, Y., Van Haren, M. J., Moret, E. E., Rood, J. J., Sartini, D., Salvucci, A., ... & Martin, N. I. (2019). Bisubstrate inhibitors of nicotinamide N-methyltransferase (NNMT) with enhanced activity. Journal of medicinal chemistry, 62(14), 6597-6614.

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For research use only. Not intended for any clinical use.

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