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NAD+

Nicotinamide adenine dinucleotide (NAD⁺, CAS 53-84-9) is an essential pyridine nucleotide coenzyme with a molecular weight of approximately 663.4 Da and formula C₂₁H₂₇N₇O₁₄P₂. Present in every living cell, NAD⁺ functions as a central electron carrier in cellular respiration (accepting hydride ions to form NADH) and as a co-substrate for NAD⁺-consuming enzymes including sirtuins, poly(ADP-ribose) polymerases (PARPs), and CD38 glycohydrolases. NAD⁺ is a cornerstone research tool in cellular metabolism, aging biology, and mitochondrial bioenergetics.

Technical Specifications

Property Value
CAS Number 53-84-9
Molecular Formula C₂₁H₂₇N₇O₁₄P₂
Molecular Weight ~663.4 Da
Purity ≥99% (HPLC-verified)
Appearance Lyophilized white powder
Solubility Highly soluble in sterile water and aqueous buffers
Storage -20°C (lyophilized), 2–8°C (reconstituted)

Mechanism of Action

NAD⁺ serves dual roles in cellular metabolism: as a redox coenzyme shuttling between oxidized (NAD⁺) and reduced (NADH) states in catabolic reactions (glycolysis, TCA cycle, β-oxidation), and as a consumable co-substrate for three major enzyme families. Sirtuins (SIRT1–7) catalyze NAD⁺-dependent deacetylation of lysine residues on histones and metabolic enzymes (e.g., PGC-1α, FOXO, p53), generating nicotinamide and 2'-O-acetyl-ADP-ribose; this links NAD⁺ availability to epigenetic regulation and mitochondrial biogenesis. PARPs cleave NAD⁺ to produce poly(ADP-ribose) chains on acceptor proteins, mediating DNA damage repair — PARP1 activation during severe DNA damage can deplete cellular NAD⁺ to near-zero levels, triggering energy crisis and necrotic cell death. CD38 and CD157 are NAD⁺ glycohydrolases that generate cyclic ADP-ribose (cADPR), a second messenger that mobilizes calcium from endoplasmic reticulum stores via ryanodine receptors. Cellular NAD⁺ levels decline with age across multiple tissues (30–50% reduction), contributing to mitochondrial dysfunction, diminished sirtuin activity, and impaired DNA repair — making NAD⁺ a central node in aging research.

Research Applications

  • Primary: Cellular metabolism and bioenergetics — redox balance, NAD⁺/NADH ratio, TCA cycle function
  • Secondary: Sirtuin biology and epigenetic regulation, DNA damage repair and PARP signaling, aging and longevity research
  • Model Systems: In vitro (all mammalian cell lines, isolated mitochondria, sirtuin activity assays), in vivo (NAD⁺ precursor supplementation models, aging and age-related disease models)

Quality Control & Analytical Methods

  • HPLC: ≥99% purity verification at 214/260 nm (C18 reversed-phase or ion-pair column)
  • Mass Spectrometry: ESI-MS for molecular weight confirmation (~663.4 ±1.0 Da)
  • Peptide Content: Not applicable (dinucleotide coenzyme); HPLC purity by area % at 260 nm
  • Endotoxin: <1 EU/mg (LAL assay)
  • TFA Content: Not applicable (non-peptide)

Stability & Storage

Condition Stability
-20°C (lyophilized) 24 months
4°C (lyophilized) 6 months
25°C (lyophilized) 1 month
Reconstituted (4°C) 7 days
Reconstituted (-20°C) 30 days

Key Research References

  • Imai & Guarente (2014) — NAD⁺ and sirtuins in aging and disease. Trends Cell Biol. PMID: 24794292
  • Canto et al. (2015) — NAD⁺ metabolism and the control of energy homeostasis: a balancing act between mitochondria and the nucleus. Cell Metab. PMID: 26187563
  • Verdin (2015) — NAD⁺ in aging, metabolism, and neurodegeneration. Science. PMID: 26676306

Source & Purchase

For researchers requiring research-grade NAD PLUS with full analytical documentation including HPLC, LC-MS, and Certificate of Analysis, visit the HK Peptides product page for specifications, bulk pricing, and ordering.

View NAD PLUS Product →

FAQ

Q: What purity level is standard for NAD+? A: HK Peptides supplies NAD⁺ at ≥99% purity by HPLC with full COA documentation.

Q: How should NAD+ be stored for research use? A: Lyophilized NAD⁺ should be stored at -20°C, protected from light and moisture. Reconstituted solutions at 4°C for short-term use (up to 7 days). Avoid repeated freeze-thaw cycles; NAD⁺ is susceptible to hydrolysis at acidic pH.