CycLex NAMPT Colorimetric Assay Kit detects nicotinamide phosphoribosyltransferase (NAMPT) activity in recombinant NAMPT or endogenous NAMPT immunoprecipitated from cell extract.
Nicotinamide phosphoribosyltransferase (NAMPT), also known as pre-B-cell colony-enhancing factor, is the rate-limiting enzyme that converts nicotinamide to nicotinamide mononucleotide (NMN) from nicotinamide in the salvage pathway of NAD+ biosynthesis in mammals. Nicotinamide mononucleotide adenylyltransferase 1 (NMNAT1) converts NMN to NAD+. The expression of NAMPT is upregulated during activation of immune cells such as monocytes, macrophages, dendritic cells, T and B cells, as well as in amniotic epithelial cells upon stimulation with several inflammatory cytokines. NAMPT-specific inhibitor, FK866 was found to deplete intracellular NAD content, resulting in apoptotic cell death in many cancer cell lines without any DNA damaging effect. Recently, Nakahata K et al, demonstrated that NAMPT is required to modulate circadian gene expression and circadian oscillation of NAD+.
CycLex NMNAT Colorimetric Assay Kit detects nicotinamide
mononucleotide adenylyltransferase (NMNAT) activity in recombinant NMNAT1 or endogenous
NMNAT1 immunoprecipitated from cell extract.
Nicotinamide mononucleotide adenylyltransferase 1 (NMNAT1) (EC 22.214.171.124) is a central enzyme in NAD biosynthesis, transferring the adenylyl moiety of ATP to nicotinamide mononucleotide (NMN) or nicotinic acid mononucleotide (NaMN) resulting in the formation of NAD or NaAD and the release of pyrophosphate. As this reaction is reversible, the enzyme may in principle be used to form ATP and NMN from NAD and pyrophosphate. This enzyme could be a potential target for therapeutical applications, because its activity is rather low in tumor cells.
Nicotinamide adenine dinucleotide (NAD+) as well as nicotinamide adenine dinucleotide phosphate (NADP+) is an important cofactor found in cells. NADH is the reduced form of NAD+, and NAD+ is the oxidized form of NADH. It has been reported that NAD+ metabolism regulates important biological effects including life span. NAD+, through poly-ADP-ribosyl polymerase (PARP), mono-ADPribosyltransferase (ARTs) and recently characterized sirtuin enzymes, exerts potential biological effects. These enzymes modify proteins to regulate their function via ADP-ribosylation or deacetylation in the presence of NAD+. These enzymes are involved in several pathways including apoptosis, DNA repair, senescence and endocrine signaling, suggesting that either the enzymes could be an important therapeutical target for cancer, diabetes atherosclerosis and so on.