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AdipoGen Life Sciences
NAPRTase (human) (rec.) (His)
Product Details | |
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Synonyms | Nicotinate Phosphoribosyltransferase; FHA-HIT-interacting Protein; FHIP; EC 2.4.2.11 |
Product Type | Protein |
Properties | |
Source/Host | E. coli |
Sequence |
Human NAPRTase is fused at the N-terminus to a His-tag. |
Crossreactivity | Human |
Biological Activity |
0.043µmol/min/mg: hNAPRTase activity was measured by a custom coupled enzymatic assay which uses a secondary enzyme for the quantification of the PRPP consumed by hNAPRTase. The reaction buffer contained 50 mM Hepes pH 7.5, 500 µM PRPP, 100 µM nicotinic acid, 20 mM MgCl2, 2.5 mM DTT and hNAPRTase at 5 µM, 25°C, spectrophotometrical monitoring. |
MW | ~58.0kDa |
Purity | ≥98% (SDS-PAGE) |
Endotoxin Content | N/A |
Concentration | 0.5mg/ml (Lot specific) |
Formulation | Liquid. In 50mM HEPES/KOH pH 7.5 containing 300mM potassium chloride and 10mM DTT. |
Other Product Data |
UniProt link Q6XQN6: NAPRTase (human) |
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. |
Documents | |
MSDS | Download PDF |
Product Specification Sheet | |
Datasheet | Download PDF |
Human nicotinate phosphoribosyltransferase (NAPRTase) is localized in the cytoplasm and is involved in biological processes such as NAD biosynthetic and metabolic processes, nicotinamide metabolic process, nicotinate nucleotide salvage, response to oxidative stress and water-soluble vitamin metabolic process. It functions by catalyzing the conversion of nicotinic acid (NA) to NA mononucleotide (NaMN) and is essential for NA to increase cellular NAD levels and prevent oxidative stress of the cells. It is a crucial factor in the NAD+ biosynthesis pathway.
Catalytic activity: Β-nicotinate D-ribonucleotide + diphosphate = nicotinate + 5-phospho-α-D-ribose 1-diphosphate.
- Characterization of human nicotinate phosphoribosyltransferase: Kinetic studies, structure prediction and functional analysis by site-directed mutagenesis: L. Galassi, et al.; Biochimie 94, 300 (2012)