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Nicotinamide Mononucleotide Adenylyltransferase 1; NMN Adenylyltransferase 1; NaMN Adenylyltransferase 1; EC 2.7.7.1
Protein
E. coli
Human full-length NMNAT1 (aa 1-279) is fused at the N-terminus to a His-tag.
Human
Well suited for the synthesis of NAD due to high specific activity and high substrate selectivity compared to NMNAT3 (human) (rec.) (His) (highly active). For NAD analog synthesis use NMNAT3 (human) (rec.) (His) (highly active) (AG-40T-0093).Note: When loss of activity is observed add 10mM DTT to the working buffer and incubate for at least 15 min before the assay.
≥5U/mg protein. One unit is defined as the amount of enzyme that synthesizes 1µmol of NAD+ per min.
~33.3kDa (monomer)
≥95% (SDS-PAGE)
N/A
~1mg/ml
Liquid. In 50mM sodium phosphate, pH8.0, containing 300mM sodium chloride, 2mM DTT and 10% glycerol.
UniProt link Q9HAN9: NMNAT1 (human)
BLUE ICE
+4°C
-20°C
After opening, prepare aliquots and store at -20°C.Avoid freeze/thaw cycles.
Working aliquots are stable for up to 3 months when stored at -20°C.
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Nuclear NMNAT isoform. 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. Interacts with PARP-1/ARTD1. Protects against axonal degeneration following mechanical or toxic insults. Widely expressed.Product References
  • Molecular cloning, chromosomal localization, tissue mRNA levels, bacterial expression, and enzymatic properties of human NMN adenylyltransferase: M. Emanuelli, et al.; J. Biol. Chem. 276, 406 (2001)
  • Characterization of recombinant human nicotinamide mononucleotide adenylyl transferase (NMNAT), a nuclear enzyme essential for NAD synthesis: M. Schweiger, et al.; FEBS Lett. 492, 95 (2001)
  • Subcellular compartmentation and differential catalytic properties of the three human nicotinamide mononucleotide adenylyltransferase isoforms: F. Berger, et al.; J. Biol. Chem. 280, 36334 (2005)
  • The NMN/NaMN adenylyltransferase (NMNAT) protein family: C. Lau, et al.; Front. Biosci. 14, 410 (2009)
  • Isoform-specific targeting and interaction domains in human nicotinamide mononucleotide adenylyltransferases: C. Lau, et al.; J. Biol. Chem. 285, 18868 (2010)