AdipoGen Life Sciences

NAD Nucleotidase (H. influenzae) (rec.)

CHF 590.00
In stock
AG-40T-0110-C05050 µgCHF 590.00
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Product Details
Synonyms NadN; NAD Pyrophosphatase/5'-nucleotidase
Product Type Protein
Source/Host E. coli
Sequence Full-length NAD 5’-nucleotidase (Haemophilus influenzae) without the signal peptide corresponding to the first 26 aa.
Biological Activity With AMP: 856.4 nmol of Ade/min/mg of protein
With NMN: 110,3 nmol of NR/min/mg of protein
With NAD: 5.4 nmol of Ade/min per mg of protein | 5.3 nmol of NR/min/mg of protein
MW ~63.0kDa
Purity ≥98% (SDS-PAGE)
Endotoxin Content N/A
Concentration 0.5mg/ml (Lot specific)
Formulation Liquid. In 5mM KH2PO4, pH 6.8 containing 100mM TRIS-HCl (pH 8.5) and 10mM MgCl2.
Other Product Data UniProt link Q4QNY4: NAD Nucleotidase (H. influenza)
Shipping and Handling
Shipping DRY ICE
Short Term Storage -20°C
Long Term Storage -80°C
Handling Advice After opening, prepare aliquots and store at -80°C.
Avoid freeze/thaw cycles.
Use/Stability Stable for at least 6 months after receipt when stored at -80°C.
MSDS Download PDF
Product Specification Sheet
Datasheet Download PDF
NadN (NAD nucleotidase) is a periplasmic enzyme from Haemophilus influenzae, a major pathogen of the respiratory tract in humans that has developed the capability to exploit host NAD(P) for its nicotinamide dinucleotide requirement. NadN plays a central role by degrading NAD into adenosine and NR (nicotinamide riboside), NMN to nicotinamide riboside and AMP to adenosine. It shows a broad substrate specificity, recognizing either mono- or di-nucleotide nicotinamides and different adenosine phosphates with a maximal activity on 5'-adenosine monophosphate. It can be used as an economically alternative to produce NR (nicotinamide riboside).
Catalytic activity: NAD=AMP + NMN=Ade+NR+PPi | AMP=Ade+Pi | NMN=NR+Pi
Product References
  1. The high-resolution crystal structure of periplasmic Haemophilus influenzae NAD nucleotidase reveals a novel enzymatic function of human CD73 related to NAD metabolism: S. Garavaglia, et al.; Biochem. J. 441, 131 (2012)
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