Recombinant Human NMNAT-2 Protein, CF

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Product Details

Summary
Reactivity HuSpecies Glossary
Applications Enzyme Activity
Format
Carrier-Free

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Recombinant Human NMNAT-2 Protein, CF Summary

Details of Functionality
Measured by the production of NAD+, which is converted to NADH by alcohol dehydrogenase. The specific activity is >1,500 pmol/min/μg, as measured under the described conditions.
Source
Spodoptera frugiperda, Sf 21 (baculovirus)-derived human NMNAT-2 protein
Met1-Glu307, with a C-terminal 6-His tag
Accession #
N-terminal Sequence
Thr2, Thr133, Thr145
Protein/Peptide Type
Recombinant Enzymes
Gene
NMNAT2
Purity
>70%, by SDS-PAGE under reducing conditions and visualized by Colloidal Coomassie® Blue stain at 5 μg per lane
Endotoxin Note
<1.0 EU per 1 μg of the protein by the LAL method.

Applications/Dilutions

Theoretical MW
35 kDa.
Disclaimer note: The observed molecular weight of the protein may vary from the listed predicted molecular weight due to post translational modifications, post translation cleavages, relative charges, and other experimental factors.
SDS-PAGE
34-38 kDa, reducing conditions
Publications
Read Publication using
6279-NT in the following applications:

Packaging, Storage & Formulations

Storage
Use a manual defrost freezer and avoid repeated freeze-thaw cycles.
  • 6 months from date of receipt, -70 °C as supplied.
  • 3 months, -70 °C under sterile conditions after opening.
Buffer
Supplied as a 0.2 μm filtered solution in Tris, NaCl, Glycerol, Brij-35 and DTT.
Purity
>70%, by SDS-PAGE under reducing conditions and visualized by Colloidal Coomassie® Blue stain at 5 μg per lane
Assay Procedure
  • Assay Buffer: 50 mM HEPES, 5 mM DTT, pH 7.5
  • Recombinant Human NMNAT‑2 (rhNMNAT-2) (Catalog # 6279-NT)
  • beta -Nicotinamide mononucleotide ( beta -NMN) (Sigma, Catalog # N3501), 50 mM stock in deionized water
  • Adenosine triphosphate (ATP) (Sigma, Catalog # A7699), 10 mM stock in deionized water
  • Yeast Alcohol Dehydrogenase (ADH) (Sigma, Catalog # A3263), 5 mg/mL stock in 25 mM MES, 20% Glycerol, pH 6.5
  • 1 M Magnesium Chloride
  • 95-100% Ethanol
  • 96-well Clear Plate (Costar, Catalog # 92592)
  • Plate reader (Model: SpectraMax Plus by Molecular Devices) or equivalent
  1. Dilute rhNMNAT-2 to 0.5 ng/µL in Assay Buffer.
  2. Prepare Substrate Mixture: 30 mM MgCl2, 1 mM beta -NMN, 4 mM ATP, 0.1 mg/mL ADH, and 2% Ethanol in 50 mM HEPES, pH 7.5.
  3. In a plate, load 50 µL of 0.5 ng/µL rhNMNAT-2, and start the reaction by adding 50 µL of Substrate Mixture to wells. Include a Substrate Blank containing 50 µL Assay Buffer and 50 µL of Substrate Mixture.
  4. Read absorbance at a wavelength of 339 nm (bottom read) in kinetic mode for 5 minutes.
  5. Calculate specific activity:

     Specific Activity (pmol/min/µg) =

Adjusted Vmax* (OD/min) x well volume (L) x 1012 pmol/mol
ext. coeff** (M-1cm-1) x path corr.*** (cm) x amount of enzyme (µg)

     *Adjusted for Substrate Blank 
     **Using the extinction coefficient 6220 M-1cm-1 
     ***Using the path correction 0.32 cm
     Note: the output of many spectrophotometers is in mOD Per Well:
  • rhNMNAT-2: 0.025 µg
  • Substrate Mixture: 0.5 mM beta -NMN, 2 mM ATP, 15 mM MgCl2, 0.05 mg/mL ADH, and 1% Ethanol

Notes

Coomassie is a registered trademark of Imperial Chemical Industries Ltd.



This product is produced by and ships from R&D Systems, Inc., a Bio-Techne brand.

Alternate Names for Recombinant Human NMNAT-2 Protein, CF

  • C1orf15
  • chromosome 1 open reading frame 15
  • EC 2.7.7.1
  • EC 2.7.7.18
  • KIAA0479MGC2756
  • NaMN adenylyltransferase 2
  • nicotinamide mononucleotide adenylyltransferase 2
  • nicotinamide nucleotide adenylyltransferase 2
  • Nicotinate-nucleotide adenylyltransferase 2
  • NMN adenylyltransferase 2
  • NMNAT2
  • NMNAT-2
  • PNAT2
  • pyridine nucleotide adenylyltransferase 2

Background

Humans produce three nicotinamide mononucleotide adenylyltransferase (NMNAT) enzymes. All three enzymes transfer adenylate from ATP to nicotinamide ribonucleotide or nicotinate ribonucleotide to generate NAD+ or deamido-NAD+, and are important enzymes in the NAD biosynthetic pathway (1). The three enzymes differ in tissue expression patterns and subcellular location, indicating that they each play a unique role in NAD homeostasis (2). NMNAT-2 is expressed primarily in the central nervous system and in muscle tissue in contrast to NMNAT-1, which has a broad tissue distribution (3). NMNAT-2 is found in the cytosol and Golgi complex, while NMNAT-1 is a nuclear enzyme and NMNAT-3 is mitochondrial (1). A number of studies have implicated the NMNAT proteins in cancer and neurodegenerative diseases (4). NMNAT‑2 has been shown to be essential for the maintenance of healthy axons. When the level of this labile protein falls below a critical threshold in axons, the process of axonal degeneration begins (5). The axon-protective function of NMNAT-2 is dependent on its NAD+ synthesis activity (6).

 

  1. Berger, F. et al. (2005) J. Biol. Chem. 280:36334.
  2. Raffaelli, N. et al. (2002) Biochem. Biophys. Res. Commun. 297:835.
  3. Yalowitz, J.A. et al. (2004) Biochem. J. 377:317.
  4. Lau, C. et al. (2009) Front. Biosci. 14:410.
  5. Gilley, J. and M.P. Coleman (2010) PLoS Biol. 8:1.
  6. Yan, T. et al. (2010) Neurochem. Int. 56:101.  

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Publications for NMNAT-2 (6279-NT)(1)

We have publications tested in 1 confirmed species: Mouse.

We have publications tested in 1 application: Immunoassay Development.


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Bioinformatics

Gene Symbol NMNAT2
Uniprot