- NADP acts as a cofactor binding to NADP-dependent enzymes, including dehydrogenases (e.g., glucose-6-phosphate dehydrogenase), reductases (e.g., glutathione reductase), and oxidases[2]

- A genetically encoded biosensor for NADP+ (derived from a NADP+-binding protein) was developed. In vitro, the biosensor showed a linear fluorescent response to NADP+ concentrations ranging from 0.1 μM to 100 μM, with high specificity (no cross-reactivity with NAD+, ATP, or GTP). The sensor’s fluorescent signal increased by ~5-fold when NADP+ concentration rose from 0.1 μM to 100 μM, enabling quantitative detection of NADP+ in buffer solutions [1]
- Recombinant NADP-dependent enzymes (e.g., malate dehydrogenase) were purified, and their binding to NADP was analyzed via X-ray crystallography. The analysis confirmed that NADP binds to the enzyme’s active site via conserved hydrogen bonds and hydrophobic interactions, with the 2'-phosphate group of NADP playing a key role in distinguishing it from NAD+ (which lacks the phosphate group) [2]

- The NADP+ biosensor was expressed in zebrafish embryos and adult mice. In zebrafish, fluorescent imaging showed dynamic changes in NADP+ levels in the liver and muscle tissues under glucose stimulation (increased NADP+ by ~2-fold at 30 min post-stimulation). In mice, intraperitoneal injection of pyruvate induced a ~1.5-fold increase in NADP+ levels in the kidney cortex, as detected by the biosensor [1]

- For intracellular NADP+ detection: HeLa cells were transfected with the biosensor plasmid via lipofection. After 24 hours of culture, cells were treated with metabolic inhibitors (e.g., 6-aminonicotinamide, an inhibitor of NADP-dependent enzymes). Fluorescent images were captured using a confocal microscope, and the fluorescent intensity was quantified to calculate intracellular NADP+ concentrations. The assay showed that 6-aminonicotinamide treatment reduced intracellular NADP+ levels by ~40% compared to the control group [1]

[1]. A genetically encoded biosensor for in vitro and in vivo detection of NADP+. Biosens Bioelectron. 2016 Mar 15;77:901-6.

[2]. NADP-dependent enzymes. I: Conserved stereochemistry of cofactor binding. Proteins. 1997 May;28(1):10-28.

[3]. The phosphate makes a difference: cellular functions of NADP. Redox Rep. 2010;15(1):2-10.

NADP zwitterion is a form of NADP. It is an important metabolite and the conjugate base of NADP(+). Nicotinamide adenine dinucleotide phosphate (NADP) is a coenzyme formed by the coupling of ribosylnicotinamide 5'-phosphate (NMN) to 5'-adenosine 2',5'-bisphosphate (A2P) via a pyrophosphate bond. It acts as an electron carrier in various reactions, alternately being oxidized (NADP+) and reduced (NADPH). (Dorland, 27th edition) NADP is a metabolite found or produced in Escherichia coli (K12 strain, MG1655 strain). It has been reported to exist in Arabidopsis thaliana, humans, and other organisms with relevant data. NADP, nicotinamide adenine dinucleotide phosphate, is a redox coenzyme present in eukaryotic cells and participates in various enzymatic reactions. Nicotinamide adenine dinucleotide phosphate (NADP) is a coenzyme formed by the coupling of ribosylnicotinamide 5'-phosphate (NMN) to adenosine 5'-phosphate 2',5'-bisphosphate via a pyrophosphate bond. It acts as an electron carrier in a variety of reactions and is alternately oxidized (NADP+) and reduced (NADPH). (Dorland, 27th edition) - NADP (nicotinamide adenine dinucleotide phosphate) exists in two forms: oxidized (NADP+) and reduced (NADPH). It is an essential cofactor in cellular redox reactions, participating in processes such as lipid synthesis, nucleotide synthesis and antioxidant defense (e.g., using NADPH to regenerate glutathione via glutathione reductase) [3] - The 2'-phosphate group of NADP is crucial to its biological function: it mediates the specific binding to NADP-dependent enzymes (preventing binding to NAD-dependent enzymes) and regulates the catalytic activity of enzymes by inducing conformational changes at the enzyme active site [2] - Genetically encoded NADP⁺ biosensors can detect NADP⁺ levels in living cells and organisms in real time and non-invasively, providing a tool for studying NADP-related metabolic pathways and diseases (e.g., metabolic disorders associated with NADP imbalance) [1] - In cells, NADP is mainly located in the cytoplasm, mitochondria and chloroplasts (in plants). The ratio of NADPH/NADP+ in the cytoplasm is maintained at approximately 100:1 to support reductive biosynthesis, while the ratio in the mitochondria is lower (approximately 7:1) to balance oxidative reactions.[3]

C21H28N7O17P3

743.41

743.075

53-59-8

53-57-6 (reduced);604-79-5 (oxidized);53-59-8 (free);1184-16-3 (Na); 100929-71-3 (ammonium); 24294-60-2 (disodium);

5885

White to off-white solid powder

-7.3

8

21

13

48

1290

8

C1=CC(=C[N+](=C1)[C@H]2[C@@H]([C@@H]([C@H](O2)COP(=O)([O-])OP(=O)(O)OC[C@@H]3[C@H]([C@H]([C@@H](O3)N4C=NC5=C(N=CN=C54)N)OP(=O)(O)O)O)O)O)C(=O)N

XJLXINKUBYWONI-NNYOXOHSSA-N

InChI=1S/C21H28N7O17P3/c22-17-12-19(25-7-24-17)28(8-26-12)21-16(44-46(33,34)35)14(30)11(43-21)6-41-48(38,39)45-47(36,37)40-5-10-13(29)15(31)20(42-10)27-3-1-2-9(4-27)18(23)32/h1-4,7-8,10-11,13-16,20-21,29-31H,5-6H2,(H7-,22,23,24,25,32,33,34,35,36,37,38,39)/t10-,11-,13-,14-,15-,16-,20-,21-/m1/s1

[[(2R,3R,4R,5R)-5-(6-aminopurin-9-yl)-3-hydroxy-4-phosphonooxyoxolan-2-yl]methoxy-hydroxyphosphoryl] [(2R,3S,4R,5R)-5-(3-carbamoylpyridin-1-ium-1-yl)-3,4-dihydroxyoxolan-2-yl]methyl phosphate

2934.99.9001

Powder      -20°C    3 years

                     4°C     2 years

In solvent   -80°C    6 months

                  -20°C    1 month

Note: This product requires protection from light (avoid light exposure) during transportation and storage.

Room temperature (This product is stable at ambient temperature for a few days during ordinary shipping and time spent in Customs)

H2O : ~250 mg/mL (~336.29 mM)
DMSO :< 1 mg/mL

Solubility in Formulation 1: 100 mg/mL (134.52 mM) in PBS (add these co-solvents sequentially from left to right, and one by one), clear solution; with sonication.

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 (Please use freshly prepared in vivo formulations for optimal results.)