NMNAT3 (human) (rec.) (His) (highly active)
| Code | Size | Price |
|---|
| AG-40T-0093-C010 | 10 ug | £200.00 |
Quantity:
| AG-40T-0093-C050 | 50 ug | £470.00 |
Quantity:
Prices exclude any Taxes / VAT
Overview
Regulatory Status: RUO
Target Species: Human
Shipping:
Blue Ice
Storage:
-20°C
Documents
Further Information
Alternate Names/Synonyms:
Nicotinamide Mononucleotide Adenylyltransferase 3; NMN Adenylyltransferase 3; NaMN Adenylyltransferase 3; EC 2.7.7.18; EC 2.7.7.1
Biological Activity:
>2U/mg protein. One unit is defined as the amount of enzyme that synthesizes 1µmol of NAD+ per min.
Concentration:
1mg/ml
EClass:
32160000
Endotoxin:
N/A
Form (Short):
liquid
Formulation:
Liquid. In 50mM TRIS-HCl, pH 8.0, containing 300mM sodium chloride, 1mM DTT and 10% glycerol.
Handling Advice:
After opening, prepare aliquots and store at -20°C.Avoid freeze/thaw cycles.
Long Description:
Protein. Human full-length NMNAT3 (aa 1-252) is fused at the N-terminus to a His-tag. Source: E. coli. Endotoxin content: N/A. Liquid. In 50mM TRIS-HCl, pH 8.0, containing 300mM sodium chloride, 1mM DTT and 10% glycerol. Purity: >95% (SDS-PAGE). Mitochondrial NMNAT isoform. Catalyzes the formation of NAD+ from nicotinamide mononucleotide (NMN) and ATP. Can also use the deamidated form of nicotinic acid mononucleotide (NAMN) as substrate with the same efficiency. Can use tiazofurin monophosphate as substrate. 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. Fails to cleave phosphorylated dinucleotides NADP+, NADPH and NAADP+. Protects against axonal degeneration following injury.
Molecular Weight:
~27kDa (monomer)
NCBI, Uniprot Number:
Q96T66
Package Type:
Plastic Vial
Product Description:
Mitochondrial NMNAT isoform. Catalyzes the formation of NAD+ from nicotinamide mononucleotide (NMN) and ATP. Can also use the deamidated form of nicotinic acid mononucleotide (NAMN) as substrate with the same efficiency. Can use tiazofurin monophosphate as substrate. 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. Fails to cleave phosphorylated dinucleotides NADP+, NADPH and NAADP+. Protects against axonal degeneration following injury.
Purity:
>95% (SDS-PAGE)
Sequence:
Human full-length NMNAT3 (aa 1-252) is fused at the N-terminus to a His-tag.
Source / Host:
E. coli
TAGs:
His
Transportation:
Non-hazardous
UNSPSC Category:
Other Enzymes
UNSPSC Number:
12352204
Use & Stability:
Working aliquots are stable for up to 3 months when stored at -20°C.
References
Structural characterization of a human cytosolic NMN/NaMN adenylyltransferase and implication in human NAD biosynthesis: X. Zhang, et al.; J. Biol. Chem. 278, 13503 (2003) | 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)