NAD+ | Laboratory Research Grade
RESEARCH MATERIAL

NAD+ | Laboratory Research Grade

Redox Coenzyme — Research Compound
$59.00
β-Nicotinamide adenine dinucleotide (NAD+) supplied as a laboratory research material for analytical, redox, and enzyme-system studies. Research use only. Not for human or veterinary use.
✓ Scientific Identity Established
⏳ Laboratory Testing In Progress
⏳ Batch Documentation Pending
✓ Research Use Only
✓ U.S. Fulfillment
In Laboratory Testing
Lot Verification Variant-specific documentation
Traceable Lots VBL lot identification
Primary Literature Peer-reviewed sources
Research Use Only Laboratory research materials

Scientific Specifications

Reference characteristics for laboratory research materials.

CAS Number
53-84-9
Purity
≥98%
Molecular Formula
C21H26N7O14P2
Molecular Weight
663.42
Appearance
White to off-white powder
Storage
-20°C
Research Classification
Research Use Only (RUO). Not for human or veterinary use.

SCIENTIFIC OVERVIEW

Scientific background and research classification for this laboratory reference material.

NAD+ (oxidized beta-nicotinamide adenine dinucleotide; CAS 53-84-9) is a dinucleotide coenzyme composed of adenine and nicotinamide nucleotides joined through their phosphate groups. It is a universal redox cofactor present in all living cells, cycling between its oxidized (NAD+) and reduced (NADH) states in central metabolism (Belenky et al., 2007).

As a laboratory reference material, NAD+ supports research into cellular redox biochemistry, energy metabolism, and the biology of NAD+-consuming enzymes. This material is supplied for laboratory research use only.

Primary Research Category
Metabolic Research
Material Type
Lyophilized Small Molecule
Intended Use
Laboratory Research
Research Categories
Energy Homeostasis Cellular Bioenergetics Mitochondrial Biology

Mechanism of Action

Molecular interaction profile describing how this research material engages receptor systems and influences downstream biological signaling pathways.

NAD+ functions as an electron-accepting coenzyme in oxidoreductase reactions and as a consumed co-substrate for NAD+-dependent enzymes. Foundational work established that the transcriptional-silencing and longevity protein Sir2 is an NAD-dependent histone deacetylase (Imai et al., 2000), defining the sirtuin family's obligate use of NAD+ as a co-substrate. Beyond redox chemistry, NAD+ pools link mitochondrial and nuclear signaling in the control of energy homeostasis (Canto et al., 2015).

Research Documentation

Laboratory documentation is presented when available for the selected product specification and current lot.

In Laboratory Testing
Laboratory Documentation In Progress

Laboratory documentation for the current lot is being completed.

Scientific References
Peer-Reviewed Literature

Explore published literature, clinical investigations, and foundational scientific research.

View References →
Laboratory Resources
Technical Guidance

Storage guidance, handling recommendations, analytical methods, and laboratory best practices.

Related Research
Companion Materials

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Research Center

Scientific literature, laboratory resources, and related materials curated to support research involving this research material.

Scientific References
Peer-Reviewed Literature

Explore curated publications from peer-reviewed journals including clinical investigations, mechanistic studies, and foundational scientific literature.

Browse References →
Scientific Dossier
Deeper Technical Treatment

Comprehensive scientific documentation including literature review, mechanism, pharmacology, and study data for this research material.

Laboratory Resources
Technical Guidance

Storage guidance, handling information, analytical standards, research policies, and laboratory support documentation.

Research Library

Curated peer-reviewed literature selected to provide scientific context for this research material.

Mechanistic Study•Nature• 2000

Transcriptional silencing and longevity protein Sir2 is an NAD-dependent histone deacetylase

Foundational study establishing that the transcriptional-silencing and longevity protein Sir2 is an NAD-dependent histone deacetylase, defining NAD+ as an obligate co-substrate for sirtuin enzymology.
Velora Research Insight
Anchors the NAD+-consuming enzyme dimension of the dossier with primary foundational evidence.
PubMed →DOI →
Review Article•Trends in Biochemical Sciences• 2007

NAD+ metabolism in health and disease

Review synthesizing NAD+ biosynthesis, salvage pathways, and coenzyme function in health and disease, anchoring the biochemical identity and metabolic roles of NAD+.
Velora Research Insight
Identity/coenzyme-function synthesis for the dossier's overview treatment.
PubMed →DOI →
Review Article•Cell Metabolism• 2015

NAD+ Metabolism and the Control of Energy Homeostasis: A Balancing Act between Mitochondria and the Nucleus

Review of NAD+ metabolism and its role in the control of energy homeostasis, linking mitochondrial and nuclear signaling through NAD+ pools.
Velora Research Insight
Consolidates the redox/bioenergetics research framework connecting NAD+ pools to energy homeostasis.
PubMed →DOI →
Preclinical Study•Science• 2016

NAD+ repletion improves mitochondrial and stem cell function and enhances life span in mice

Preclinical study demonstrating that NAD+ repletion improves mitochondrial and stem-cell function in mice, establishing NAD+ availability as a central variable in metabolic research models.
Velora Research Insight
Primary preclinical anchor for the cellular/metabolic research context; presented as research context, not a therapeutic representation.
PubMed →DOI →