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Research Use Only. Not for human or veterinary use. Third-party HPLC tested · Batch-verifiable COAs.
NAD+ — 1000 mg research vial, >99% HPLC purity
Longevity & Mitochondrial

NAD+

Nicotinamide adenine dinucleotide • Cellular energy research

NAD+ (nicotinamide adenine dinucleotide) is a central coenzyme in cellular energy metabolism and a key reference compound in longevity and mitochondrial research.

$160.00
Size

SKU: PRC-NAD-1000

Research Use Only. Not for human or veterinary use. By ordering you confirm you are a qualified researcher.

Purity Verification

HPLC Purity

>99% HPLC

Mass Spec Verified

ESI-MS

Certificate of Analysis

Per batch

Preparation & Handling

Supplied as lyophilized powder. Store unreconstituted vials at -20 °C, protected from light. Reconstitute with bacteriostatic or sterile water; once reconstituted, store at 2–8 °C and use within the validated stability window. Do not freeze-thaw repeatedly. For laboratory research use only.

The Science Behind NAD+

NAD+ (nicotinamide adenine dinucleotide) is one of the most fundamental molecules in cell biology — an electron carrier in energy metabolism and a consumable co-substrate for a family of signalling enzymes. Its decline with age and the strategies used to restore it are a central theme of modern geroscience. The summaries below describe that literature with citations, for research context only; this material is supplied for in-vitro and laboratory use, not for human or veterinary use.

Overview

NAD+ (nicotinamide adenine dinucleotide) is a coenzyme present in all living cells. It is central to energy metabolism both as an electron carrier in redox reactions — cycling between NAD+ and NADH across glycolysis, the TCA cycle, and oxidative phosphorylation — and as a co-substrate consumed by a set of signalling enzymes. [1]

Mechanism: redox vs. signalling pools

A key distinction in the literature is between NAD+'s catalytic redox role (where it is recycled, not consumed) and its role as a substrate that is degraded by non-redox enzymes. The latter links NAD+ availability directly to downstream signalling, because every signalling reaction lowers the cellular NAD+ pool. [2]

NAD+-consuming enzymes

Three enzyme families consume NAD+: the sirtuins (NAD+-dependent deacylases tied to gene regulation and mitochondrial function), the poly(ADP-ribose) polymerases (PARPs, central to DNA-damage repair), and the NADase CD38. [2] Their shared dependence on NAD+ means these pathways compete for a common, limited pool — a concept widely used to interpret metabolic and DNA-repair research. [1]

Decline with age & geroscience

Cellular NAD+ availability falls with age across many tissues, an observation that has made NAD+ metabolism a major focus of geroscience. Reviews describe associations between declining NAD+, increased CD38 activity, cellular senescence, and several biological hallmarks of aging. [3]

NAD+-boosting strategies

A large body of work examines whether raising NAD+ — through precursors such as nicotinamide mononucleotide (NMN) and nicotinamide riboside (NR), or through enzyme modulation — affects metabolic and age-related endpoints in model systems. The in-vivo evidence for these NAD-boosting molecules has been systematically reviewed. [4]

Research-use context

These materials are supplied strictly for in-vitro and laboratory research by qualified professionals. Nothing in the summaries above is a therapeutic claim, and the compound is not formulated, dosed, or authorised for use in humans or animals.

Research Use Only. The information above is provided for educational and reference purposes only and summarizes third-party laboratory and preclinical research. Peptide Research Center products are intended solely for in-vitro and laboratory research by qualified professionals — not for human or veterinary use, diagnosis, or treatment. Nothing here constitutes medical advice or a therapeutic claim.

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