NAD+ 1,000mg

Compound Name: Nicotinamide adenine dinucleotide (NAD+)

Synonyms: β-Nicotinamide adenine dinucleotide, NAD, Diphosphopyridine nucleotide, Coenzyme I, Nadide

Molecular Formula: C₂₁H₂₇N₇O₁₄P₂

Molecular Weight: ~663.43 g/mol

Structure: Synthetic coenzyme

Peptide Sequence: N/A; not a peptide

Chemical Structure:

Source: PubChem

Mechanism of Action: NAD⁺ functions as an essential electron carrier by cycling between oxidized (NAD⁺) and reduced (NADH) forms in cellular metabolism, accepting and donating electrons during glycolysis, the TCA cycle, and oxidative phosphorylation to support ATP production. Beyond its redox coenzyme activity, NAD⁺ serves as a substrate for sirtuins, poly(ADP-ribose) polymerases (PARPs), and other signaling enzymes that consume NAD⁺ during the processes of DNA repair, deacetylation, and cellular stress response. These enzymatic reactions profoundly influence energy homeostasis, repair capacity, cellular stress resistance, and gene expression

Biological Activity: NAD⁺ is indispensable for over 400 cellular reactions, supports mitochondrial function, and modulates antioxidant defenses. Its levels directly impact metabolic health, aging processes, DNA repair, and cellular resilience to stress^1,2. NAD⁺ depletion, as seen in aging and certain diseases, is linked to mitochondrial dysfunction, impaired oxidative metabolism, and decreased repair capacity^3,4.

Storage: Store at -20°C or below, protected from light and moisture.

Drug Categories: Coenzymes, Redox agents, Energy metabolism intermediates

Additional Notes: NAD⁺ is not a peptide; it is a dinucleotide formed from nicotinamide and adenine via a pair of ribose-phosphate linkers

Summary Table:

Disclaimer: For Research Use Only. Not intended for human or veterinary use. This compound is supplied solely for laboratory and R&D purposes.

Detailed Product Description

Nicotinamide adenine dinucleotide (NAD⁺) is an essential molecule found in all living cells, acting at the crossroads of energy metabolism and cellular signaling. As a coenzyme, NAD⁺ participates in redox reactions critical for ATP production by shuttling electrons during glycolysis, the TCA cycle, and oxidative phosphorylation. Besides its cofactor role, NAD⁺ is also a substrate for NAD⁺-consuming enzymes such as sirtuins (regulators of gene expression and longevity pathways) and PARPs, which mediate DNA repair and cellular stress responses. Declines in NAD⁺ levels are associated with aging, metabolic dysfunction, and neurodegeneration, making NAD⁺ replenishment and boosting strategies of growing scientific and clinical interest. Unlike synthetic peptides or hormones, NAD⁺ is a naturally occurring nucleotide-derived molecule, and its manipulation can influence cell vitality, resilience, and repair capacity^1,2,3.

Research Highlights

• Cellular NAD⁺ depletion with age or disease may impair energy metabolism and increase vulnerability to stress^3,4.
• NAD⁺ supplementation and precursor therapy (e.g., NR, NMN) potentially restore NAD⁺ pools and improve cellular function³.

• Widely used in metabolism, aging, and neurobiology research; not for therapeutic or veterinary use unless otherwise specified.

Mechanism of Action

Nicotinamide adenine dinucleotide (NAD⁺) serves as a central metabolic cofactor and essential substrate for a number of intracellular enzymes that regulate critical biological processes. Its mechanism of action is primarily mediated by its role as a substrate for NAD⁺-dependent enzymes such as the sirtuin family (SIRT1-7), poly(ADP-ribose) polymerases (PARPs), and certain ectoenzymes like CD38 and CD157. Sirtuins utilize NAD⁺ to catalyze deacetylation and ADP-ribosylation reactions, thereby modulating gene expression, metabolism, and stress resistance in a manner tightly linked to cellular NAD⁺ availability. PARPs, on the other hand, respond to DNA damage by using NAD⁺ to generate ADP-ribose polymers, which are essential for DNA repair and maintaining genome stability; overactivation of PARPs, such as during extensive genotoxic stress, can result in significant NAD⁺ depletion and subsequent compromise of cellular energy homeostasis. CD38 and CD157 act as multifunctional ectoenzymes that metabolize NAD⁺ to produce signaling molecules like ADP-ribose and cyclic ADP-ribose, which are involved in calcium signaling and immune regulation. In neurons, the enzyme SARM1 is rapidly activated under conditions of metabolic stress or axonal injury, triggering swift NAD⁺ cleavage and initiating axonal degeneration. Collectively, NAD⁺ exerts its effects not through traditional receptor binding but through its indispensable role as a co-substrate and regulator of these enzymatic systems, which sense and respond to fluctuations in NAD⁺ levels to coordinate cellular metabolism, survival, DNA repair, signaling, and cell fate decisions^1-4.

Pharmacokinetic Profile:

• Route of Administration: Intravenous, Oral
• Dosing Frequency: Once daily
• Half-Life: The precise plasma half-life of exogenously administered NAD⁺ in humans is not well characterized in the literature. However, available human studies indicate that NAD⁺ is rapidly cleared from the plasma for at least the first two hours of infusion, reflecting immediate tissue uptake and/or metabolism.

Formulation & Handling

• Lyophilized powder, reconstituted in sterile saline.
• Store lyophilized powder at –20 °C; Reconstituted solution cannot be stored.

Selected Clinical Trial Activity

References

¹Huang, Q., Sun, M., Li, M., Zhang, D., Han, F., Wu, J. C., Fukunaga, K., Chen, Z., & Qin, Z.-H. (2018). Combination of NAD+ and NADPH offers greater neuroprotection in ischemic stroke models by relieving metabolic stress. Molecular Neurobiology, 55, 6063–6075.

²Grant, R., Berg, J., Mestayer, P. N., Braidy, N., Bennett, C., Broom, G. M., & Watson, K. (2019). A pilot study investigating changes in the human plasma and urine NAD+ metabolome during a 6 hour intravenous infusion of NAD+. Frontiers in Aging Neuroscience, 11, 257.

³Ying, W. (2013). Roles of NAD+, PARP-1, and sirtuins in cell death, ischemic brain injury, and synchrotron radiation X-ray-induced tissue injury. Scientifica, 2013, 691251.

⁴Yoshino, J., Baur, J. A., & Imai, S. I. (2018). NAD+ intermediates: the biology and therapeutic potential of NMN and NR. Cell Metabolism, 27, 513–528.