Nicotinamide adenine dinucleotide (NAD+) is a ubiquitous pyridine nucleotide coenzyme found in all living cells and is among the most extensively studied metabolic cofactors in contemporary biochemist...
Certificate of Analysis included with every order.
Technical Specifications
Purity
≥98%
Form
Lyophilized powder
Storage
-20°C
Molecular Weight
663.43 Da
Sequence
C₂₁H₂₇N₇O₁₄P₂
CAS Number
53-84-9
About This Peptide
Nicotinamide adenine dinucleotide (NAD+) is a ubiquitous pyridine nucleotide coenzyme found in all living cells and is among the most extensively studied metabolic cofactors in contemporary biochemistry. Catalogued under CAS 53-84-9 and carrying the internal code NAD+, this compound presents as a lyophilized powder of ≥98% purity with a molecular weight of 663.43 Da and the molecular formula C₂₁H₂₇N₇O₁₄P₂. It consists of two nucleotides — adenosine monophosphate and nicotinamide mononucleotide — joined via a pyrophosphate bridge, forming a dinucleotide that cycles between its oxidized (NAD+) and reduced (NADH) states during enzymatic redox reactions.
Nicotinamide adenine dinucleotide occupies a central position in cellular energy metabolism, serving as an electron carrier in glycolysis, the tricarboxylic acid cycle, and the mitochondrial electron transport chain. Beyond its canonical role in redox biochemistry, NAD+ functions as a critical substrate for a growing class of NAD+-consuming enzymes, including sirtuins (class III histone deacetylases), poly(ADP-ribose) polymerases (PARPs), and cyclic ADP-ribose synthases such as CD38 and CD157. This substrate-level regulatory function has positioned NAD+ at the intersection of research into DNA damage response, epigenetic regulation, and intracellular calcium signaling.
Research interest in nicotinamide adenine dinucleotide has intensified significantly over the past two decades, driven in part by observations that cellular NAD+ concentrations decline with organismal age and in models of metabolic dysfunction. These findings have prompted extensive in vitro and preclinical investigations into the consequences of NAD+ depletion and the effects of experimental repletion on various cellular parameters. The compound is supplied as a lyophilized powder for convenient reconstitution in aqueous research buffers and should be stored at −20°C to maintain integrity. For research use only. Not for human consumption.
Research Applications
≥98% purity. Lyophilized powder. Storage: -20°C. For research purposes only.
Mechanism of Action
In its primary biochemical role, NAD+ accepts a hydride ion (H⁻) from substrate molecules during catabolic oxidation reactions, becoming reduced to NADH. This redox cycling is catalyzed by a broad range of NAD+-dependent dehydrogenases — including lactate dehydrogenase, malate dehydrogenase, and the multienzyme complexes of the mitochondrial respiratory chain — thereby coupling substrate oxidation to downstream ATP synthesis via oxidative phosphorylation. The ratio of NAD+ to NADH is a quantifiable indicator of cellular redox status and is commonly used as a readout in metabolic flux studies.
Beyond redox catalysis, NAD+ serves as a co-substrate that is stoichiometrically consumed by sirtuin deacylases (SIRT1–7), which cleave the glycosidic bond of NAD+ to generate nicotinamide and O-acetyl-ADP-ribose alongside the deacetylated protein product. This reaction links NAD+ availability directly to sirtuin-mediated post-translational modification of histones, transcription factors, and mitochondrial proteins. PARP enzymes similarly consume NAD+ to synthesize poly(ADP-ribose) chains on target proteins in response to DNA strand breaks, while CD38 hydrolyzes NAD+ to produce the second messenger cyclic ADP-ribose, implicating NAD+ in calcium-dependent signaling cascades. Collectively, these pathways make intracellular NAD+ concentration a key variable in studies of gene expression regulation, genomic stability, and organelle biogenesis.
Research Applications
Nicotinamide adenine dinucleotide is employed across a range of in vitro and preclinical research contexts, particularly in studies requiring precise manipulation or measurement of cellular NAD+ pools. Representative research application areas include:
Enzymatic activity assays: Use as a cofactor or substrate standard in spectrophotometric and fluorometric assays measuring NAD+-dependent dehydrogenase and oxidoreductase kinetics.
Sirtuin biochemistry: Substrate supplementation in cell-free and cell-based systems to investigate SIRT1–7 deacylase activity, protein acetylation states, and downstream transcriptional effects.
DNA damage and PARP research: Provision of exogenous NAD+ in models of genotoxic stress to study poly(ADP-ribosyl)ation dynamics and PARP-mediated DNA repair pathways.
Metabolic flux and bioenergetics studies: Quantification and perturbation of the NAD+/NADH ratio in isolated mitochondria or cultured cells to characterize oxidative phosphorylation and glycolytic capacity.
Aging and senescence models: Supplementation of NAD+ in cellular senescence and age-related model systems to examine the impact of cofactor availability on mitochondrial function and gene expression profiles.
CD38/calcium signaling research: Substrate provision for in vitro CD38 enzyme assays and for investigating cyclic ADP-ribose-mediated intracellular calcium mobilization.
Storage & Handling Guidelines
Proper storage and handling are essential to maintain peptide integrity and ensure reliable research results. All Pepitiva Biolabs peptides are supplied as lyophilized (freeze-dried) powder, which provides excellent long-term stability when stored correctly. Store lyophilized peptides at -20°C for long-term storage or 2-8°C for short-term use. Once reconstituted, peptide solutions should be stored at 2-8°C and used within the timeframe specified in the product documentation. Always use sterile bacteriostatic water for reconstitution and handle peptides in a clean laboratory environment to prevent contamination. Avoid repeated freeze-thaw cycles, as thermal stress can cause peptide degradation and loss of biological activity.
Quality Control & Certification
This product is manufactured under strict quality control protocols and has been verified through comprehensive analytical testing. Each batch undergoes reverse-phase HPLC analysis for purity determination and electrospray ionization mass spectrometry (ESI-MS) for molecular identity confirmation. A detailed Certificate of Analysis (COA) is available for download, documenting purity percentage, molecular weight verification, appearance, and recommended storage conditions. Pepitiva Biolabs maintains batch-level traceability from synthesis through delivery, ensuring complete transparency and quality assurance for your research.
Frequently Asked Questions
Is this product approved for human use?
No. This product is intended exclusively for in vitro scientific research and laboratory use. It is not approved for human or veterinary use, not intended for diagnostic or therapeutic purposes, and should not be administered to humans or animals under any circumstances.
How do I reconstitute this peptide?
Add sterile bacteriostatic water slowly to the vial, directing the stream against the glass wall rather than directly onto the lyophilized powder. Gently swirl the vial until the powder is fully dissolved — do not shake vigorously. The recommended reconstitution volume depends on your desired concentration. Refer to the product documentation for specific guidance.
Can I get a Certificate of Analysis (COA)?
Yes. A Certificate of Analysis is included with every order and is also available for download from the product page. The COA documents HPLC purity, mass spectrometry identity confirmation, batch number, production date, and storage recommendations.
For research use only. Not for human consumption.
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