NAD+ Peptide | NAD+ 100mg
NAD+ 1000mg is a high-purity, research-grade compound supplied in lyophilized (freeze-dried) solid form, intended exclusively for laboratory and research use. Produced under rigorous quality control, this compound offers exceptional stability and consistency for analytical testing and in vitro research.
NAD+ Peptide Information
| Property | Value |
| Name | NAD+ |
| CAS Number | 53-84-9 |
| Molecular Formula | C21H27N7O14P2 |
| Molecular Weight | 663.4 g/mol |
| PubChem CID | 5892 |
| Synonyms | nadide, 53-84-9, Nicotinamide Adenine Dinucleotide, coenzyme I, beta-NAD, Codehydrogenase I |
| Vial Size | NAD+ 100mg, NAD+ 500mg, NAD+ 1000mg |
| Purity (HPLC) | ≥99.0% |
NAD+ Peptide Features
- Strict Research Designation: Formulated specifically to support in vitro laboratory evaluation, life science research, and biochemical assays.
- Lyophilized Matrix Stability: Provided as a highly stable, lyophilized powder to preserve structural integrity during transit and minimize baseline degradation.
- Rigorous Analytical Purity: Produced under stringent quality controls in order to achieve outstanding chemical purity, verified via high-performance liquid chromatography (HPLC) and mass spectrometry (MS).
- Mitochondrial and Enzymatic Research: It serves as an ideal cofactor in studies involving sirtuins, poly(ADP-ribose) polymerases (PARPs) and electron transport chain dynamics.
- Precision Temperature Requirements: Requires sub-zero storage upon receipt to preserve molecular stability and avoid hydrolysis.
- Moisture-Resistant Packaging: Packed in special, airtight glass vials to prevent moisture ingress and extend shelf-life of chemicals.
Product Overview
Studying cell energetics, enzyme regulation and metabolic homeostasis requires stable and high-purity biochemical cofactors. Nicotinamide Adenine Dinucleotide (NAD+ Peptide) has long been an integral reagent within life science research laboratories and molecular biology laboratories as a critical coenzyme involved in oxidation-reduction reactions such as glycolysis, citric acid cycle or mitochondrial electron transport chain electron acceptor processes.
At its discovery and structural elucidation in the early 20th century, Nicotinamide Adenine Dinucleotide revolutionized scientific understanding of cellular fermentation and metabolic pathways. Early biochemical investigations established its role as a heat-stable cofactor that laid the groundwork for modern bioenergetics. As years progressed, laboratory interest expanded from its role in foundational metabolism towards its requirement as an enzyme substrate in various enzyme families such as sirtuins and poly(ADP-ribose) polymerases (PARPs).
Current laboratory researchers use NAD+ research products like these lyophilized NAD+ compounds for studying cell signaling cascades, DNA repair mechanisms and enzyme kinetics. Due to its highly stable composition and rigorous analytical specifications for manufacturing purposes, investigators can establish precise baseline concentrations within controlled experimental models with this product. As chemical integrity can directly influence quantitative assay validity, this product has been produced so as to minimize degradation products which might confound results and therefore remain a standard reagent in academic, institutional and biotechnology laboratories globally.
What is NAD+?
Nicotinamide Adenine Dinucleotide (NAD+) is an ubiquitous coenzyme located in all living cells. Structurally, it is a dinucleotide consisting of two mononucleotides linked through their phosphate teams: one nucleotide includes an adenine base, while the other has a nicotinamide ring.
[Nicotinamide] – [Ribose] – [Phosphate] – [Phosphate] – [Ribose] – [Adenine]
The primary biochemical duty of NAD+ is to facilitate electron transfer within metabolic pathways. It alternates between its oxidized kind (NAD+) and its reduced kind (NADH), acting as a crucial metabolic shuttle.

NAD molecule.. Source: Getty Images
Discovery History and Scientific Significance
1906: Discovered by British biochemists Arthur Harden and William John Young throughout research studies on the fermentation of sugar by yeast juice.
1936: German biochemist Otto Heinrich Warburg showed the feature of the nicotinamide moiety in hydrogen transfer responses during redox procedures.
Modern Age: Study shifted towards understanding its role past electron transport, particularly as a signaling molecule and a derogatory substrate for enzymes regulating chromatin framework and cellular stress and anxiety reactions.
In scientific exploration, preserving an in-depth understanding of this particle’s structural kinetics allows scientists to model mobile actions to numerous metabolic conditions, making it a vital possession in contemporary biochemistry and biology.
NAD+ IN Scientific Research
In modern life science research laboratories, Study Usage NAD+ is extensively made use of to map complicated biochemical networks and cellular communications. Scientist release this substance across numerous distinctive approach locations:
1. Cellular Research and Bioenergetics
Investigators make use of NAD+ to control the redox state of in vitro cell cultures. By changing the baseline ratio of NAD+ to NADH, researchers can observe changes in mitochondrial membrane layer capacity, oxygen usage rates, and glycolytic flux. These studies give foundational insight right into exactly how cells adapt to modifications in nutrition schedule and outside stressors.
2. Enzymatic Assays and Kinetics
NAD+ functions as an obligate substratum for several courses of enzymes:
Sirtuins (SIRT1-SIRT7): NAD+- dependent deacetylases that regulate genetics expression and metabolic homeostasis.
PARPs (Poly( ADP-ribose) Polymerases): Enzymes involved in the cellular reaction to DNA damages.
CD38/157: Ectoenzymes that manufacture secondary carriers from NAD+.
By presenting regulated concentrations of high-purity NAD+ into cell-free systems, scientists can determine maximum response rates (Vmax) and Michaelis constants (Kilometres) for these enzymes.
3. Experimental Laboratory Methodology
When creating protocols involving NAD+, scientists have to thoroughly control variables such as pH, temperature, and barrier composition. Since the nicotinamide ring is vulnerable to nucleophilic attack and hydrolysis, preserving rigorous experimental criteria is crucial to preventing spontaneous non-enzymatic cleavage throughout testing cycles.
Scientific Background
To understand the wider scientific literary works context surrounding NAD+, it is essential to review its placement within cellular biochemistry and biology. The particle runs at the junction of power manufacturing and genomic upkeep.
In the mitochondrial matrix, the reduction of NAD+ to NADH is coupled with the oxidation of carbon substratums derived from carbs and lipids. The succeeding contribution of electrons from NADH to Facility I of the electron transport chain drives the proton gradient essential for ATP synthesis through oxidative phosphorylation. The essential formula governing this relatively easy to fix redox reaction is:

Beyond these timeless redox couples, ongoing scientific examinations concentrate heavily on the usage of NAD+ by non-redox enzymes. In these pathways, the particle is cleaved right into nicotinamide and an ADP-ribosyl piece. Because this procedure completely eats the particle, cellular systems need to continuously replenish it using salvage, afresh, or Preiss-Handler synthesis pathways.
Researchers often study these synthesis networks in lab versions to observe just how cells keep steady-state degrees under varying experimental difficulties. Assessing these paths adds to the cumulative scientific knowledge pertaining to standard mobile feature, cellular aging models, and molecular survival systems under stress and anxiety.
STORAGE AND HANDLING GUIDELINES
Proper NAD+ Storage and meticulous laboratory handling are critical to preventing degradation and ensuring experimental reproducibility. Lyophilized compounds are highly sensitive to environmental factors, and failure to follow established protocols can lead to sample degradation.
Temperature Control: Upon receipt, store the lyophilized product in a calibrated freezer at -20℃ for short-to-medium-term storage, or -80℃ for long-term preservation. Avoid frost-free freezers, as temperature fluctuation cycles can introduce thermal stress.
Moisture and Reconstitution Protection: The lyophilized powder is highly hygroscopic. Prior to reconstitution, allow the vial to equilibrate to room temperature inside a desiccator or dry environment. This prevents the condensation of atmospheric moisture onto the product upon opening.
Light Mitigation: Store vials in their original packaging or an amber container shielded from direct light exposure, as prolonged ultraviolet radiation can destabilize the nicotinamide ring structure.
Aliquot Selection: Following reconstitution in an appropriate sterile laboratory buffer, divide the solution into single-use aliquots. Freeze these aliquots immediately at -80℃ to prevent repeated freeze-thaw cycles, which accelerate hydrolytic cleavage.
FREQUENTLY ASKED QUESTIONS
What is NAD+?
Nicotinamide Adenine Dinucleotide (NAD+) is a coenzyme present in all living cells that acts as a primary electron carrier in cellular redox reactions and serves as an essential substrate for enzymes regulating cellular processes.
How should NAD+ be stored?
For optimal preservation, store the lyophilized powder at -20℃ or -80℃ in a stable, non-frost-free freezer, protected completely from light and moisture.
Is NAD+ a peptide?
Technically, NAD+ is a dinucleotide coenzyme rather than a peptide, as it is composed of nucleotides linked by phosphate groups rather than an amino acid sequence joined by peptide bonds. However, it is frequently categorized alongside research peptides within life science distribution channels due to similar handling, lyophilization methods, and research application spaces.
What does research-use-only mean?
Research-use-only signifies that the compound is manufactured exclusively for in vitro laboratory experimentation, scientific evaluations, and academic research. It is completely prohibited from human or animal consumption, therapeutic administration, or diagnostic procedures.
What laboratory fields study NAD+?
NAD+ is actively studied across multiple disciplines, including molecular biology, cellular bioenergetics, biochemistry, mitochondrial genetics, and enzymatic kinetics.
Can this product be used in vivo?
No. This product is prepared strictly for in vitro laboratory research, chemical assays, and controlled cellular cultures. It is not formulated, sterile-tested, or authorized for in vivo animal or human administration.
Why is NAD+ supplied in a lyophilized form?
Lyophilization removes water content while preserving the molecular structure. This process significantly improves the compound’s chemical stability during shipping and extends its overall shelf life when kept under recommended storage conditions.
What buffers are recommended for reconstitution?
NAD+ is readily soluble in sterile water or standard laboratory aqueous buffers, such as phosphate-buffered saline (PBS) or Tris-HCl, depending on the specific requirements of your downstream assay.
RESEARCH NOTES
Laboratory Context: This product profile serves purely educational and informational purposes for the scientific community. All data provided regarding NAD+ Peptide are compiled from peer-reviewed biochemical literature.
Regulatory Notice: This substance is categorized solely as a laboratory reagent. It must not be utilized as a medical treatment, diagnostic tool, dietary supplement, or drug. All handling must be performed by trained laboratory personnel inside controlled research environments.
SCIENTIFIC REFERENCES
For comprehensive peer-reviewed literature and chemical databases regarding Nicotinamide Adenine Dinucleotide, researchers are encouraged to consult the following authoritative repositories:
- Peer-Reviewed Journals: The Journal of Biological Chemistry, Cell Metabolism, and Trends in Biochemical Sciences.
- Scientific Databases: PubChem (CID 5892), ChemSpider, and the Kyoto Encyclopedia of Genes and Genomes (KEGG).
- Institutional Resources: The National Institutes of Health (NIH) Molecular Biology databases and the International Union of Biochemistry and Molecular Biology (IUBMB).
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⚠ Intended Use
All products are intended for in vitro laboratory research use only.
They are strictly prohibited for administration to humans or animals, and must not be used for diagnostic, therapeutic, or clinical applications.
Storage and Handling
Store lyophilized powder at –20°C.
After reconstitution (for laboratory analysis), store at 2–8°C.
Avoid repeated freeze-thaw cycles.
Maintain aseptic technique during handling.







