NMNAT3, human recombinant protein
Nicotinamide Mononucleotide Adenylyl-transferase 3; NMN Adenylyltransferase 3; NaMN Adenylyltransfer
|Calculated MW||~27.0 kDa (monomer). Human full-length NMNAT3 (aa 1-252) is fused at the N-terminus to a His-tag.|
|Other Names||Nicotinamide Mononucleotide Adenylyl-transferase 3; NMN Adenylyltransferase 3; NaMN Adenylyltransferase 3; EC 220.127.116.11; EC 18.104.22.168|
|Results||≥ 2U/mg protein. One unit is defined as the amount of enzyme that synthesizes 1 µmol of NAD+ per min.|
|Storage||-20°C; 1 mg/ml in 50 mM sodium phosphate, pH 8.0 containing 300 mM sodium chloride, 1 mM DTT and 10% glycerol.|
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Provided below are standard protocols that you may find useful for product applications.
This is the Mitochondrial NMNAT isoform. It catalyzes the formation of NAD+ from nicotinamide mononucleotide (NMN) and ATP. It can also use the deamidated form of nicotinic acid mononucleotide (NAMN) as substrate with the same efficiency. It can use tiazofurin monophosphate as substrate. It can also use GTP and ITP as nucleotide donors. Also catalyzes the reverse reaction, i.e. the pyrophosphorolytic cleavage of NAD+. For the pyrophosphorolytic activity, mitochondrial NMNAT isoform can use NAD (+), NADH, NAAD, nicotinic acid adenine dinucleotide phosphate (NHD), nicotinamide guanine dinucleotide (NGD) as substrates. It fails to cleave phosphorylated dinucleotides NADP+, NADPH and NAADP+. It protects against axonal degeneration following injury.
Wang Y.-G.,et al.Submitted (FEB-2001) to the EMBL/GenBank/DDBJ databases.
Ota T.,et al.Nat. Genet. 36:40-45(2004).
Muzny D.M.,et al.Nature 440:1194-1198(2006).
Mural R.J.,et al.Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
Berger F.,et al.J. Biol. Chem. 280:36334-36341(2005).
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