NMNAT1 Protein, Human (sf9, His)

The NMNAT1 protein catalyzes the formation of NAD(+) from NMN and ATP and efficiently uses deamidated NaMN and triazofurane monophosphate as substrates. NMNAT1 Protein, Human (sf9, His) is the recombinant human-derived NMNAT1 protein, expressed by Sf9 insect cells , with C-His labeled tag. The total length of NMNAT1 Protein, Human (sf9, His) is 279 a.a., with molecular weight of ~34 kDa.

The NMNAT1 protein assumes a pivotal role in cellular processes as it catalyzes the formation of NAD(+) from nicotinamide mononucleotide (NMN) and ATP. Moreover, it exhibits comparable efficiency in utilizing the deamidated form, nicotinic acid mononucleotide (NaMN), as a substrate and can employ triazofurin monophosphate (TrMP) in the same capacity. Additionally, NMNAT1 catalyzes the reverse reaction, the pyrophosphorolytic cleavage of NAD(+), with a preference for NAD(+) and NaAD as substrates, displaying lesser efficiency in degrading NADH, nicotinic acid adenine dinucleotide phosphate (NHD), and nicotinamide guanine dinucleotide (NGD). Beyond its role in NAD(+) biosynthesis, NMNAT1 is involved in nuclear ATP generation, collaborating with PARP1, PARG, and NUDT5, a process essential for energy-demanding chromatin remodeling events. Furthermore, it serves as a cofactor for glutamate and aspartate ADP-ribosylation, directing PARP1 catalytic activity to histone residues. Notably, NMNAT1's enzymatic activity fails to cleave phosphorylated dinucleotides NADP(+), NADPH, and NaADP(+). Functionally, NMNAT1 plays a crucial role in protecting against axonal degeneration in response to mechanical or toxic insults.

Human

Sf9 insect cells

C-His

Q9HAN9 (M1-T279)

64802  [NCBI]

Approximately 34 kDa

Greater than 95% as determined by reducing SDS-PAGE or Tris-Bis PAGE.

Lyophilized powder

Lyophilized from a 0.2 μm filtered solution of 20 mM Tris, 500 mM NaCl, 3 mM DTT, 10% Glycerol, pH 7.4. Normally 5 % - 8 % trehalose, mannitol and 0.01% Tween 80 are added as protectants before lyophilization.

<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.