NAD+ (Nicotinamide Adenine Dinucleotide) — Cellular Energy, Longevity & DNA Repair Research Compound | Klene Peptides
For Research Use Only | Not for Human or Veterinary Administration
Nicotinamide Adenine Dinucleotide (NAD+) is a fundamental coenzyme present in every living cell, serving simultaneously as the primary electron carrier in cellular energy metabolism and as an essential substrate for a broad class of regulatory enzymes — including all seven sirtuins, PARP DNA repair enzymes, and the cyclic ADP-ribose signaling enzyme CD38. NAD+ levels decline progressively with aging, by approximately 50% between young adulthood and middle age in many tissues — a decline now recognized as a central driver of age-related metabolic dysfunction, impaired DNA repair, mitochondrial deterioration, and reduced cellular stress resilience. Research into NAD+ restoration and its downstream signaling effects spans neurodegeneration, cardiovascular aging, metabolic disease, cancer biology, and longevity, making it one of the most broadly studied research compounds in biogerontology. Klene Peptides supplies NAD+ to USA research institutions with verified purity and same-day fulfillment.
Every vial from Klene Peptides includes:
- ≥99%+ purity — verified by HPLC (High-Performance Liquid Chromatography)
- HPLC-MS (High-Performance Liquid Chromatography - Mass Spectrometry)
- Same-day shipping for all USA orders
Chemical Identity & Structural Profile
| Parameter | Value |
|---|---|
Full Name | Nicotinamide Adenine Dinucleotide (oxidized form) |
Abbreviation | NAD⁺ |
Chemical Class | Dinucleotide coenzyme |
Molecular Formula | C₂₁H₂₇N₇O₁₄P₂ |
Molecular Weight | 663.43 g/mol (free acid form) |
CAS Number | 53-84-9 |
Structure | Adenine nucleotide + nicotinamide nucleotide linked via phosphoanhydride bridge |
Redox Pair | NAD⁺ (oxidized) / NADH (reduced) |
Biological Occurrence | All living cells; cytoplasm, mitochondria, nucleus |
Appearance | White to off-white lyophilized powder |
Solubility | Water, PBS; prepare fresh aqueous solutions |
Storage | Lyophilized: −20°C, protected from light and moisture; Reconstituted: use within 24 hours |
NAD+ exists in two functional states: the oxidized NAD+ form, which accepts electrons to become NADH during cellular respiration, and the reduced NADH form, which donates electrons at Complex I of the electron transport chain. Beyond its electron carrier role, NAD+ is consumed and depleted by regulatory enzymes as a co-substrate — meaning cellular NAD+ concentration is a dynamic, rate-limiting variable in multiple physiological processes simultaneously.
Mechanism of Action
Energy Metabolism
| Metabolic Pathway | NAD+ Role | Effect |
|---|---|---|
Glycolysis | Electron acceptor (glyceraldehyde-3-phosphate dehydrogenase) | Drives glucose-to-pyruvate ATP generation |
TCA Cycle (Krebs Cycle) | Electron acceptor (multiple dehydrogenases) | NADH generation for oxidative phosphorylation |
Oxidative Phosphorylation | NADH donates electrons at Complex I | ATP synthesis via electron transport chain |
Beta-Oxidation (fatty acids) | NADH generation from acyl-CoA processing | Fatty acid energy utilization |
Sirtuin Activation (Longevity Signaling)
All seven sirtuins require NAD+ as a co-substrate — consuming it during deacetylation reactions — making sirtuin activity directly rate-limited by cellular NAD+ availability:
| Sirtuin | Localization | Key Function |
|---|---|---|
SIRT1 | Nucleus | Gene silencing (histone deacetylation), p53 regulation, mitochondrial biogenesis via PGC-1α |
SIRT2 | Cytoplasm | Tubulin deacetylation; cell cycle progression |
SIRT3 | Mitochondria | Mitochondrial protein deacetylation; ROS reduction |
SIRT4 | Mitochondria | ADP-ribosyltransferase; fatty acid oxidation regulation |
SIRT5 | Mitochondria | Desuccinylase; urea cycle enzyme regulation |
SIRT6 | Nucleus | DNA repair; telomere maintenance; NF-κB regulation |
SIRT7 | Nucleolus | rRNA transcription regulation |
DNA Repair (PARP Pathway)
| Enzyme | Function | NAD+ Dependence |
|---|---|---|
PARP-1 | Detects and responds to DNA single-strand breaks | Consumes NAD+ to synthesize poly-ADP-ribose (PAR) at damage sites |
PARP-2 | DNA damage response redundancy | NAD+-dependent |
SIRT6 | Double-strand break repair coordination | NAD+-dependent histone deacetylase |
CD38 & NAD+ Consumption
CD38 is the dominant NAD+-consuming enzyme in most mammalian tissues, generating cyclic ADP-ribose (cADPR) for calcium signaling. CD38 expression increases with age and chronic inflammation, accelerating age-associated NAD+ decline. CD38 inhibition as a NAD+ restoration strategy is under active research investigation.
Pharmacokinetic & ADME Profile
| Parameter | Value | Notes |
|---|---|---|
Molecular Weight | 663.43 g/mol | IV provides most direct cellular delivery |
Routes (Research) | IV, IP, SC, oral (precursor comparison studies) | IV studied extensively for acute repletion |
Bioavailability (IV) | Near 100% | Direct systemic delivery |
Plasma Half-Life | ~1–2 hours (IV) | Rapid cellular uptake and enzymatic interconversion |
Cellular Uptake | Active transport via CD73/equilibrative nucleoside transporters | Enzymatic dephosphorylation + membrane transport |
Distribution | All tissues; highest concentrations in liver, kidney, brain | Universal metabolic requirement |
Metabolism | Interconverts to NADH, NMN, nicotinamide via enzymatic cycling | Nampt and NMNAT-dependent biosynthetic cycle |
Precursor Relationship | NMN and NR are biosynthetic precursors to NAD+ | Precursor bioavailability vs. direct NAD+ compared in research |
Research Applications
Aging & Longevity
| Research Area | Observed Effect | Key Mechanism |
|---|---|---|
Healthspan extension (C. elegans, mice) | Extended lifespan and healthspan markers | SIRT1, SIRT3; mitochondrial biogenesis |
Muscle aging and sarcopenia | Improved muscle function; mitochondrial density restoration | SIRT1/PGC-1α axis |
Cognitive aging | Improved memory and neuroplasticity markers | SIRT1; BDNF upregulation |
Metabolic aging | Improved insulin sensitivity; reduced adiposity | SIRT1, SIRT3, AMPK cross-talk |
Neurodegeneration Research
| Disease Model | NAD+ Role | Research Direction |
|---|---|---|
Alzheimer’s disease | Reduced brain NAD+ in AD; SIRT1/SIRT3 neuroprotection | PARP inhibition; NAD+ repletion studies |
Parkinson’s disease | Mitochondrial Complex I support; SIRT3-mediated protection | Mitochondrial quality control |
Traumatic brain injury | PARP-mediated NAD+ depletion post-injury | NAD+ restoration as neuroprotective strategy |
Multiple sclerosis | Axonal degeneration linked to NAD+/SIRT1 decline | Neuroprotection and remyelination models |
Cardiovascular Research
- SIRT3-mediated mitochondrial antioxidant defense in cardiomyocytes
- Reduced cardiac inflammation via SIRT1/NF-κB axis
- Improved post-ischemic recovery in NAD+-replete models
- CD38-driven NAD+ decline in aging cardiac tissue under active investigation
Metabolic Disease
- NAD+/SIRT1-driven hepatic fatty acid oxidation
- Pancreatic beta-cell protection through PARP inhibition reducing oxidative cell death
- Glucose homeostasis improvement via mitochondrial function restoration
- Type 2 diabetes models: NAD+ repletion and insulin secretion improvement
Cancer Biology
- PARP inhibitors (which preserve NAD+ by preventing PARP-mediated depletion) are FDA-approved cancer therapies
- SIRT6-dependent suppression of tumor glycolysis (Warburg effect)
- Cancer cell NAD+ dependence as a therapeutic vulnerability under investigation
Research Dosing Reference
For scientific reference only — not prescriptive recommendations
| Research Model | Reported Dose | Route | Duration |
|---|---|---|---|
Longevity (rodent dietary supplementation) | 300–500 mg/kg/day | Dietary / water | 3–12 months |
Acute metabolic studies | 10–100 mg/kg | IP, SC | Acute/subacute |
Neurological injury models | 50–100 mg/kg | IP | Acute administration |
Cell culture assays | 0.1–10 mM (extracellular) | Cell culture media | Per experiment |
IV infusion (clinical pilot reference) | 250–500 mg (flat dose) | IV | 4–8 hours per session |
Ranges derived from PMC-indexed preclinical and preliminary clinical research.
Reconstitution Reference
| Amount | Sterile Water | Concentration |
|---|---|---|
250 mg | 5.0 mL | 50 mg/mL |
500 mg | 10.0 mL | 50 mg/mL |
Klene Peptides Quality Standards
Certificate of Analysis — Standard Parameters
Every batch supplied by Klene Peptides is verified against the following analytical benchmarks:
| Test | Specification | Method |
|---|---|---|
Purity | ≥99% | HPLC (High-Performance Liquid Chromatography) |
Molecular Identification | Confirmed | HPLC-MS (High-Performance Liquid Chromatography – Mass Spectrometry) |
Water Content | <1.5% | — |
What Every Klene Peptides Order Includes
- Lot-specific Certificate of Analysis traceable to synthesis batch
- Verified cold-chain shipping — all orders dispatched with appropriate cold-pack packaging
- Same-day fulfillment — orders placed before cutoff ship the same business day
Ordering NAD+ for Your Research Program
Important Research Compliance Notice
Scientific References
- Verdin E. "NAD+ in aging, metabolism, and neurodegeneration." Science. 2015;350(6265):1208-1213.
- Rajman L, Chwalek K, Sinclair DA. "Therapeutic Potential of NAD-Boosting Molecules: The In Vivo Evidence." Cell Metabolism. 2018;27(3):529-547.
- Yoshino J, Baur JA, Imai SI. "NAD+ Intermediates: The Biology and Therapeutic Potential of NMN and NR." Cell Metabolism. 2018;27(3):513-528.
- Cantó C, et al. "NAD+ Metabolism and the Control of Energy Homeostasis." Cell Metabolism. 2015;22(1):31-53.
- Imai S, Guarente L. "NAD+ and sirtuins in aging and disease." Trends Cell Biol. 2014;24(8):464-471.
- Gomes AP, et al. "Declining NAD+ Induces a Pseudohypoxic State Disrupting Nuclear-Mitochondrial Communication during Aging." Cell. 2013;155(7):1624-1638.
- PubChem. NAD+. CID: 5893. https://pubchem.ncbi.nlm.nih.gov