NAD+

Overview

Torsena supplies buffered research-grade NAD+ to qualified laboratories across the European Union. Specifically, this product is lyophilized nicotinamide adenine dinucleotide co-formulated with sodium bicarbonate. Therefore it reconstitutes directly to physiological pH, roughly 7.0 to 7.4, without any titration step. Furthermore, we hold stock in Europe, so orders ship without intra-EU customs delay.

Lot & Supply Format

• Formulation. NAD+ co-lyophilized with sodium bicarbonate buffer.
• Presentation. Lyophilized powder, sealed in glass research vials.
• Quantities. Single vials as standard, though we also quote bulk on request.
• Documentation. Batch-specific CoA available on request.
• Shipping. Dispatched from Europe, and always with temperature-appropriate packaging.

What is NAD+ (Buffered)?

NAD+ is a pyridine nucleotide coenzyme that appears in more than 500 enzymatic reactions. Primarily it carries electrons through glycolysis, the citric acid cycle, and oxidative phosphorylation. Consequently it sits at the centre of cellular energy metabolism.

Beyond redox chemistry, three enzyme families consume NAD+ as a substrate. These are the sirtuins, which are NAD+-dependent deacylases, the PARPs, which handle DNA repair, and CD38 together with CD157, which synthesise cyclic ADP-ribose. Notably, all three compete for the same intracellular pool, and that competition is itself a research subject.

Why the buffered format matters. Pure NAD+ reconstitutes acidic, typically around pH 3.0 to 4.0. That acidity degrades the compound and interferes with sensitive assays. Therefore most researchers titrate before use, which adds a step and introduces variability. This product arrives pre-buffered instead, so it reconstitutes at physiological pH directly.

Supplied exclusively for in-vitro and ex-vivo research by qualified laboratories. Not intended for human or animal administration.

Buffered vs Unbuffered NAD+

Unbuffered preparations require manual pH adjustment. However, titration introduces run-to-run variation, and it costs preparation time. Buffered NAD+ removes both problems, since co-lyophilization with sodium bicarbonate fixes the pH at the point of manufacture rather than at the bench.

Consequently the buffered format suits several situations particularly well.

• Enzymatic assays. Consistent pH matters, and therefore so does a consistent starting point.
• Cell culture and metabolic studies. Routine work where an extra prep step adds no value.
• High-throughput workflows. Preparation time compounds across plates.
• Reproducibility-critical work. Namely anywhere assay-to-assay variance is the limiting factor.
• Labs without pH infrastructure. Otherwise titration means buying equipment.

Spectrophotometric Reference Values

Most NAD+ work measures the coenzyme optically, so the absorbance constants matter more than almost any other parameter.

The 340 nm figure for NADH is the one you will use most. Because NAD+ does not absorb meaningfully at 340 nm while NADH does, that wavelength tracks the oxidation state directly. Therefore dehydrogenase assays follow the reaction as a change in A340, and 6220 M⁻¹cm⁻¹ converts that change into concentration. Expressed per millimolar, the same constant reads 6.22, so a 1 mM NADH solution gives an absorbance of 6.22 through a 1 cm path.

Note that the 260 nm values carry more variation across the literature than the 340 nm figure does. Therefore treat them as approximate, and prefer 340 nm wherever the assay allows.

Mechanistic Overview

Redox coenzyme function. NAD+ accepts a hydride ion to become NADH during catabolism. NADH then donates electrons to the mitochondrial electron transport chain, and ATP synthesis follows. Consequently the NAD+/NADH ratio serves as a direct readout of cellular energy status, and researchers track it in metabolic flux and mitochondrial function work.

Sirtuin substrate. All seven mammalian sirtuins require NAD+ as a co-substrate. Moreover, availability is rate-limiting, so NAD+ concentration becomes the variable that governs sirtuin activity. Therefore it features heavily in work on gene regulation, metabolic adaptation, and stress response.

PARP substrate. PARPs consume NAD+ during poly-ADP-ribosylation in the DNA damage response. Since sirtuins and PARPs draw from the same pool, competition between them acts as a regulatory mechanism in its own right. Studies examine this under genotoxic stress, particularly where energy allocation is the question.

CD38 substrate. CD38 and CD157 hydrolyse NAD+ into cyclic ADP-ribose and nicotinamide. Notably, CD38 expression rises with age in experimental models. As a result researchers treat it as a major driver of age-related NAD+ decline, and therefore as a target in longevity work.

Published Research Data

Key references:
Cantó C, Menzies KJ, Auwerx J. NAD+ metabolism and the control of energy homeostasis: a balance of power between mitochondria and the nucleus. Cell Metab. 2015;22(1):31-53.
Verdin E. NAD+ in aging, metabolism, and neurodegeneration. Science. 2015;350(6265):1208-1213.
Camacho-Pereira J, et al. CD38 dictates age-related NAD decline and mitochondrial dysfunction through an SIRT3-dependent mechanism. Cell Metab. 2016;23(6):1127-1139.
Rajman L, Chwalek K, Sinclair DA. Therapeutic potential of NAD-boosting molecules: the in vivo evidence. Cell Metab. 2018;27(3):529-547.

Reconstitution & Storage

NAD+ dissolves readily in water, unlike most peptides. Therefore reconstitution is straightforward.

• Solvent. Deionized water or a low-ionic-strength buffer.
• pH. No adjustment needed, since the buffered format reconstitutes at roughly 7.0 to 7.4.
• Stability. Sensitive to alkaline conditions and to heat, so avoid both.
• Short-term storage. 2-8°C.
• Long-term storage. Aliquot, then freeze at -20°C.
• Freeze-thaw. Avoid repeated cycles, because each one costs integrity.

Keep lyophilized material at -20°C. Furthermore, let vials warm to room temperature before opening, since condensation otherwise introduces moisture. Otherwise follow your institutional SOPs for handling lyophilized cofactors.

NAD+ research compound specifications

Analytical Documentation

We provide batch-specific documentation on request for institutional procurement. Typically it covers three areas.

• Identity. UV-Vis confirmation, namely the characteristic A260 absorption.
• Composition. HPLC analysis by small-molecule method.
• Physical checks. Appearance, and likewise solubility verification.

Why Choose Torsena for Buffered NAD+

• Ready to use. Pre-buffered, so reconstitution needs no titration step.
• Documentation. We send batch CoAs on request.
• EU distribution. We ship from European stock, and therefore intra-EU orders clear no customs.
• Direct contact. You reach the team directly, rather than a ticket queue.

Frequently Asked Questions

What is the extinction coefficient of NADH at 340 nm?
NADH has a molar extinction coefficient of 6220 M⁻¹cm⁻¹ at 340 nm. Expressed per millimolar that is 6.22, so a 1 mM solution reads an absorbance of 6.22 through a 1 cm path. Because NAD+ does not absorb meaningfully at 340 nm, this wavelength tracks the oxidation state directly.

Why use buffered NAD+ instead of standard NAD+?
Pure NAD+ reconstitutes acidic, typically around pH 3.0 to 4.0, and that acidity degrades the compound while interfering with sensitive assays. Therefore unbuffered material needs titration before use. Buffered NAD+ reconstitutes at physiological pH directly, so it removes both the extra step and the variability that comes with it.

What is the molecular weight of NAD+?
NAD+ weighs 663.43 g/mol, and its formula is C21H27N7O14P2. The CAS number is 53-84-9 and the PubChem CID is 925.

How should you store NAD+?
Keep lyophilized material at -20°C, sealed, and away from light. Store reconstituted solution at 2-8°C for short-term use, or aliquot and freeze at -20°C otherwise. Furthermore, avoid alkaline conditions and heat, since NAD+ degrades under both.

Which enzymes consume NAD+?
Three families draw on the same pool. Sirtuins use it as a co-substrate for deacylation, PARPs consume it during DNA repair, and CD38 with CD157 hydrolyse it into cyclic ADP-ribose. Notably that shared dependence means competition between the three is itself a regulatory mechanism.

Related Research Compounds

Researchers working on cellular energy metabolism and mitochondrial function usually look at these three as well.

• MOTS-c. A mitochondrial-derived peptide, particularly for AMPK and exercise mimetic research.
• SS-31. A mitochondria-targeted peptide, and therefore relevant to cristae integrity and bioenergetics work.
• GHK-Cu. A copper tripeptide, namely for gene expression and regeneration research.

Otherwise, browse the full catalog at the Torsena shop.