NAD+ vial 1000 mg

NAD+ (nicotinamide-adenine-dinucleotide) is a naturally occurring coenzyme, chemically a dinucleotide composed of a nicotinamide and an adenine nucleotide. In scientific research, it is studied as a model compound for redox biochemistry and enzyme kinetics and as a reference standard in analytical work. This compound is offered as a freeze-dried powder of 1000 mg per vial, exclusively for laboratory and research purposes.

What is NAD+?

NAD+ (β-nicotinamide-adenine-dinucleotide) is a dinucleotide in which two ribonucleotides are joined via their 5′-phosphate groups to form a pyrophosphate bridge: an adenine ribonucleotide on one side and a nicotinamide ribonucleotide with a positively charged pyridinium ring on the other. This asymmetric structure—a recognizable adenosine region next to a redox-active pyridinium ring—makes the compound a widely used model in the study of cofactor recognition, binding site geometry, and electron transfer.

In research models, NAD+ functions as a reversible hydride acceptor: the nicotinamide ring accepts a hydride ion at position C4, resulting in the reduced form NADH. This NAD+/NADH couple forms the basis of numerous in vitro enzyme assays, because the conversion can be monitored spectrophotometrically by the characteristic absorption of NADH at 340 nm. Additionally, NAD+ is studied in cell models as a co-substrate for NAD+-consuming enzymes such as sirtuins, poly(ADP-ribose) polymerases, and CD38, which cleave the glycosidic bond between nicotinamide and ADP-ribose, thereby releasing nicotinamide. Consequently, NAD+ is used as a model compound and reference substance within scientific research.

Research areas

In a laboratory context, NAD+ occurs in the following research areas, among others:

• Enzyme kinetic study of NAD+-dependent dehydrogenases, in which the NAD+/NADH couple is spectrophotometrically monitored in vitro.
• Research into NAD+-consuming enzymes (sirtuins, poly(ADP-ribose)polymerases, CD38) and their co-substrate dependence in cell-free systems.
• Biochemical model studies of the salvage pathway and the enzymes NAMPT and NMNAT involved in the formation of dinucleotide cofactors.
• Redox biochemistry and structure-activity research on pyridine nucleotides and their structural analogs.
• Analytical method development and validation (HPLC, LC-MS) using NAD+ as the reference standard.
• Stability and solubility studies of freeze-dried nucleotide cofactors under controlled conditions.

Each of these applications involves controlled laboratory or preclinical model research.

NAD+ within our research range

NAD+ falls under the category of freeze-dried investigational compounds in vial form within our product range. While NAD+ is being investigated as a co-enzyme and co-substrate in enzymatic and redox-oriented systems, other components within the same product line have been specifically selected to cover receptor-bound or signal transduction-oriented targets. These compounds share the freeze-dried form and vial packaging but differ fundamentally in molecular class and investigated mechanism.

Specifications

Shape, handling and storage

NAD+ is supplied as a freeze-dried, white to off-white powder with a standardized quantity of 1000 mg per vial. Unlike a solid tablet form, the lyophilisate is intended to be dissolved in a suitable solvent prior to analytical work; the choice of that solvent and the concentration used depend entirely on the analytical protocol of the laboratory itself.

Store the vial refrigerated, protected from direct light and moisture, in the original packaging. The dinucleotide is sensitive to moisture and repeated temperature changes. Handle the compound with standard laboratory precautions: work in a clean environment, use appropriate personal protective equipment, and prevent cross-contamination with other research materials. Keep the packaging out of reach of unauthorized persons.

Composition and lab results

This lyophilisate is manufactured with a controlled purity of ≥ 99% (HPLC). The vial contains the compound as a dry powder without added excipients, making the material suitable as a reference material in analytical applications.

You can find an overview of the available analytical documentation on our lab results pageThe reports are collected centrally there, so that you can incorporate the data into your own research records.

Frequently Asked Questions

To which substance class does NAD+ belong?
NAD+ is not a peptide, but a dinucleotide coenzyme: two ribonucleotides (adenine and nicotinamide) connected by a pyrophosphate bridge. It therefore contains no amino acid sequence and belongs to the class of pyridine nucleotide cofactors.

What is the difference between NAD+ and NADH in research?
NAD+ is the oxidized form and NADH the reduced form of the same molecule. In vitro, the nicotinamide ring at position C4 accepts a hydride ion, producing NADH. Because only NADH absorbs strongly at 340 nm, this conversion can be directly monitored spectrophotometrically in enzyme analysis.

In what form is the connection supplied?
As a freeze-dried powder of 1000 mg in a sealed vial, without added excipients. The powder is dissolved in a suitable solvent in a laboratory setup before being used analytically.

How do I store the vial?
Refrigerated, protected from light and moisture, preferably unopened in the original packaging. Avoid repeated temperature changes.