Peptide Insider Research Desk · Handling & Storage series · Reviewed against primary literature indexed in PubMed · All content is strictly for research reference; not for human or veterinary use.
β-Nicotinamide adenine dinucleotide (NAD+; CAS 53-84-9; ChEBI:15846; C21H27N7O14P2, 663.4 g/mol) is a pyridine dinucleotide, not a peptide, yet it is catalogued beside peptides by nearly every research-reagent vendor, and the resulting search vocabulary is a tangle of formulation descriptors, fill-mass tokens and category errors. Queries such as nad+ buffered, nad buffered vs unbuffered, nad+ reconstitution, peptide nad+, nad500, lyophilized nad+ and nad+ 1000 mg all resolve to the same oxidised dinucleotide but ask different chemical questions. This review, a companion to our NAD+ compound review, addresses the chemistry behind those questions: why the free acid dissolves to an acidic solution, why NAD+ is stable in acid and labile in alkali (and NADH the reverse), how buffer anions themselves accelerate hydrolysis, and how the lyophilised fill masses on catalogue labels should be read. A 48-row crosswalk then maps each query variant to its canonical referent and to an explicit research-use-only scope status.
Definition box. Unbuffered NAD+ denotes the lyophilised free acid: dissolution in water yields an acidic solution (approximately pH 3 at the concentrations typical of research stock solutions) because the pyrophosphate bridge carries dissociable protons. Buffered NAD+ denotes a presentation co-lyophilised with a base, most often sodium bicarbonate or supplied as the sodium salt, so that dissolution yields a solution near neutral pH. The descriptor refers to the solid-state formulation, not to a different molecule.
1. Entity Anchoring: What "NAD+" Denotes in a Research Catalogue
NAD+ is composed of a nicotinamide ring attached through an N-glycosidic bond to ribose, which is joined by a pyrophosphate bridge to a second ribose bearing adenine. Its central roles in redox chemistry (as the NAD+/NADH couple), in sirtuin deacylation, in poly(ADP-ribose) polymerase signalling and in CD38-mediated cyclic-ADP-ribose formation are reviewed by Cantó, Menzies and Auwerx[1] and by Covarrubias and colleagues[2]. Mammalian cells maintain the pool chiefly by salvage: nicotinamide is converted to nicotinamide mononucleotide (NMN) by nicotinamide phosphoribosyltransferase (NAMPT)[12], and NMN is adenylylated to NAD+, with the pathway distributed across cytosolic, nuclear and mitochondrial compartments[13]. Isotope-tracer flux work by Liu and colleagues quantified whole-body synthesis-breakdown rates in mice and showed that most tissues turn the pool over within hours[15], a kinetic point that matters when reading any culture-model result.
The catalogue-category confusion is structural: research vendors list NAD+ alongside peptides because both are shipped as lyophilised powders in septum vials, and search engines inherit the juxtaposition. The tokens peptide nad+, peptide nad plus, nad plus peptides, nad+ research peptide, nad+500mg peptide and the vowel-transposed nad peotide therefore carry a category error rather than a different compound. The direct questions is nad plus a peptide and is nad + a peptide have an unambiguous answer: no. A peptide is a chain of α-amino acids joined by amide bonds; NAD+ contains no amino acid residues and no amide backbone (the nicotinamide carboxamide is a ring substituent, not a peptide bond). Co-listing queries such as nad and peptides and peptides and nad are recorded here as terminology only.
2. Acid–Base Behaviour: Why the Free Acid Is Acidic and Why It Matters
The two phosphate groups of the pyrophosphate bridge each carry a dissociable proton in the free acid. When the lyophilised free acid is dissolved in unbuffered water, those protons are released and the solution is acidic. This is the origin of the catalogue distinction encoded in nad+ buffered vs unbuffered and nad+ vs nad+ buffered: the "buffered" presentation has been co-formulated with a base so that the reconstituted solution sits near neutral pH. The molecule itself is unchanged; what differs is the counter-ion and the pH of the resulting solution.
The stability consequence is counter-intuitive and well documented. Lowry, Passonneau and Rock established in 1961 that the oxidised pyridine nucleotides (NAD+, NADP+) are stable in acid and destroyed in alkali, whereas the reduced forms (NADH, NADPH) are stable in alkali and destroyed in acid[3]. The alkali-labile site of NAD+ is the N-glycosidic bond between nicotinamide and ribose; hydroxide attack at the pyridinium ring initiates cleavage that releases nicotinamide and ADP-ribose. Bernofsky isolated 2'-phosphoadenosine diphosphate as an alkali-degradation product of the phosphorylated analogue NADP+, confirming that the adenosine-phosphate half survives while the nicotinamide half is lost[8]. Conversely, Burton and Kaplan characterised the acid-modification product of NADH[5], and Johnson and Tuazon resolved the mechanism as acid-catalysed hydration across the 5,6-double bond of the dihydronicotinamide ring[6]. The pH window that protects NAD+ therefore destroys NADH, which is the reason the co-listing query 5 amino 1mq with nadh cannot be answered with a single handling rule: the two redox states have opposite pH requirements.
A second, less widely appreciated finding is that the buffer species itself participates. Anderson and Anderson reported in 1963 that NAD+ hydrolysis at a given alkaline pH is accelerated by the buffer anions present, with rate constants that depend on buffer identity and concentration, consistent with general-base or nucleophilic catalysis at the pyridinium ring[4]. Wu, Wu and Knight later quantified the same dependence for NADPH, showing degradation kinetics governed jointly by pH, temperature and buffer composition[7]. Chenault and Whitesides, reviewing cofactor regeneration for synthetic chemistry, summarised the practical envelope: NAD+ is most persistent in mildly acidic, cool, buffer-lean solution, while NADH prefers the mildly alkaline side[9]. In research-reagent terms, an unbuffered NAD+ solution is chemically the more stable stock; a buffered solution trades some intrinsic stability for pH compatibility with enzyme assays and culture media that cannot tolerate an acidic spike.
3. Buffered vs Unbuffered: The Formulation Trade-off Stated Precisely
The questions what is nad+ buffered and what is buffered nad+ can now be answered in one sentence: buffered NAD+ is a lyophilised co-formulation of β-NAD+ with a base (sodium bicarbonate or sodium hydroxide neutralisation to the sodium salt) chosen so that reconstitution yields a near-neutral solution. The trade-off summarised in the table below follows directly from the stability literature cited above. Neither presentation is "better" in the abstract; the choice depends on whether the downstream research system is pH-sensitive (favouring buffered) or whether long-lived stock solution is the priority (favouring unbuffered free acid stored cold). Manning and colleagues' general framework for lyophilised biologic stability, covering moisture, excipient glass-transition and pH memory in the dried cake, applies equally to small-molecule cofactor cakes[10].
| Attribute | Unbuffered β-NAD+ (free acid) | Buffered β-NAD+ (sodium salt / bicarbonate co-lyophilisate) | Primary source |
|---|---|---|---|
| Solution pH on dissolution in water | Acidic (≈ pH 3 at research stock concentrations) | Near neutral (≈ pH 6.5–7.5, formulation-dependent) | Chemistry of the pyrophosphate free acid |
| Intrinsic NAD+ hydrolysis rate | Lowest (acid-stable regime) | Higher (approaches alkali-labile regime; buffer anions catalyse) | Lowry 1961[3]; Anderson 1963[4] |
| Compatibility with pH-sensitive assays / media | Requires separate neutralisation | Direct | Chenault & Whitesides 1987[9] |
| Effect on NADH if both are present | Acid regime degrades NADH | Neutral regime tolerates NADH | Burton & Kaplan 1963[5]; Johnson & Tuazon 1977[6] |
| Lyophilised-cake considerations | Single-component cake | Bicarbonate can evolve CO2 on dissolution; sodium content added | Manning 2010[10] |
| Mass basis on label | Free-acid mass | Verify whether label mass is free-acid equivalent or salt mass | Analytical practice; Trammell & Brenner 2013[11] |
4. Fill-Mass Nomenclature: Reading "nad500", "nad+ 1000 mg" and Their Variants
Research catalogues label lyophilised NAD+ vials by nominal fill mass, and search vocabulary compresses those labels into tokens: nad500 and nad+500 (compound fused to mass, unit dropped), nad + 500 mg (spaces inserted around the charge symbol), and the explicit ladder nad 50mg, nad 200 mg, nad 750 mg, nad+ 1000 mg and 1000 mg nad. Two points of chemistry govern how these labels should be read. First, fill mass is a quantity of solid, not a concentration and not a use instruction; the concentration of a reconstituted solution is simply the fill mass divided by the diluent volume added, and the handling queries nad+ reconstitution, nad+ 500 mg reconstitution, nad 500 mg reconstitution, 500mg nad+ reconstitution, nad+ 1000mg reconstitution, how to reconstitute nad+ 500 mg, how to reconstitute 500mg nad+ and reconstituting nad+ 500mg all reduce to that arithmetic plus the pH considerations in Section 2. This review does not issue reconstitution protocols; it records the chemistry that any protocol must respect. Second, for buffered presentations the label may state salt mass rather than free-acid equivalent, a difference of roughly 3–7% depending on the counter-ion, which is why analytical confirmation by LC-MS is the arbiter of true content[11].
The descriptor lyophilized nad+ names the physical state in which the reagent is shipped. Freeze-drying removes bulk water and arrests hydrolysis; the dried cake's residual moisture and pH memory determine how quickly degradation resumes after reconstitution[10]. Diluent choice interacts with the formulation: the water grades, preservative content and acetic-acid co-solvents relevant to any lyophilised research reagent are surveyed in our bacteriostatic water and reconstitution media review, and vial-transfer consumables in the laboratory syringes and needles review. Neither of those articles, nor this one, addresses administration.
5. Evidence Table: What the Located Literature Actually Measures
| Study | Research Model | Signal Vector | Relevance to the buffered/unbuffered question |
|---|---|---|---|
| Lowry et al. 1961[3] | Purified pyridine nucleotides in defined acid/alkali solutions | Residual nucleotide by enzymatic cycling assay vs time, pH, temperature | Establishes the opposite pH stability of NAD+ and NADH |
| Anderson & Anderson 1963[4] | NAD+ in a series of buffers at alkaline pH | Pseudo-first-order hydrolysis rate constants vs buffer identity and concentration | Shows buffer anions themselves catalyse hydrolysis |
| Bernofsky 1975[8] | Alkali-treated NADP+ | Chromatographic isolation and identification of degradation products | Identifies the adenosine-phosphate fragment surviving alkali cleavage |
| Burton & Kaplan 1963[5]; Johnson & Tuazon 1977[6] | NADH and analogues in acid | UV spectral shift, kinetic isotope and pH-rate profiles | Defines the acid-hydration pathway that destroys reduced forms |
| Wu et al. 1986[7] | NADPH in clinical-assay buffers | Degradation kinetics vs pH, temperature, buffer | Quantitative template for buffer-dependent cofactor stability |
| Chenault & Whitesides 1987[9] | Cofactor regeneration systems (review) | Compiled half-lives of NAD+/NADH under synthetic conditions | Practical stability envelope for stock solutions |
| Trammell & Brenner 2013[11] | Yeast and mammalian extracts | Targeted LC-MS quantitation of NAD+ metabolome | Analytical method for verifying reagent content and purity |
| Revollo 2004[12]; Nikiforov 2011[13] | Mammalian cell lines | NAMPT-dependent salvage; compartmentalised biosynthesis from extracellular precursors | Context for how cells handle exogenous NAD+ and precursors |
| Camacho-Pereira 2016[14] | Wild-type vs CD38-knockout mice; tissue lysates | NAD+ levels, CD38 NADase activity, SIRT3 targets | Identifies CD38 as a major NAD+-consuming enzyme in vivo |
| Liu et al. 2018[15] | Isotope-tracer infusion in mice | Synthesis-breakdown fluxes by LC-MS | Whole-body turnover kinetics of the NAD+ pool |
| Ratajczak 2016[18]; Grozio 2019[19] | NRK1-knockout cells and mice; Slc12a8 transport assays | Precursor (NMN/NR) utilisation and transport | Explains why intact extracellular NAD+ and its precursors behave differently |
| Airhart 2017[20]; Clement 2019[21] | Human plasma and blood metabolomics (observational) | Blood NAD+ metabolite levels | Analytical baselines for the plasma NAD+ metabolome; no formulation conclusions |
Reviews by Yoshino, Baur and Imai[16] and by Rajman, Chwalek and Sinclair[17] compile the preclinical literature on NAD+ precursors; both are cited here for context only, and neither addresses the buffered/unbuffered formulation question directly. No located study compares buffered and unbuffered NAD+ presentations head-to-head in any biological model, and this review makes no claim that the formulation difference produces any biological difference.
6. Query-Notation Crosswalk: 48 Variants, One Dinucleotide
Each search variant below is classified by the mechanism that generated it (formulation descriptor, handling term, fill-mass token, category error, co-listing, route or commercial modifier), mapped to its canonical referent and assigned an explicit research-use-only scope status. Rows marked Declined are recorded as vocabulary only and receive no substantive answer here.
| Query variant (verbatim) | Class | Generating mechanism | Canonical referent | RUO scope status |
|---|---|---|---|---|
| nad+ buffered | Formulation descriptor | Catalogue distinguishes a co-lyophilised sodium-bicarbonate / sodium-salt presentation from the free acid | β-NAD+, sodium salt or bicarbonate co-lyophilisate | Recorded – formulation terminology |
| buffered nad+ | Formulation descriptor | Word-order inversion of the above | β-NAD+, buffered presentation | Recorded – formulation terminology |
| nad+ buffered vs unbuffered | Comparison query | Two catalogue presentations compared on pH and stability | Free acid (acidic solution) vs neutral-pH co-lyophilisate | Recorded – formulation comparison (chemistry only) |
| nad buffered vs unbuffered | Comparison query | Charge symbol dropped | Same referent as row above | Recorded – formulation comparison (chemistry only) |
| nad+ vs nad+ buffered | Comparison query | Free acid explicitly contrasted with buffered form | β-NAD+ free acid vs buffered β-NAD+ | Recorded – formulation comparison (chemistry only) |
| what is nad+ buffered | Definition query | Question form of the formulation descriptor | Defined in Section 3 | Recorded – formulation terminology |
| what is buffered nad+ | Definition query | Question form, inverted word order | Defined in Section 3 | Recorded – formulation terminology |
| nad+ buffered peptide | Category error + formulation | 'Peptide' appended by catalogue-section metonymy | β-NAD+ (dinucleotide; not a peptide) | Recorded – category corrected |
| nad+ reconstitution | Handling descriptor | Generic dissolution of the lyophilised solid | Dissolution in a defined diluent volume | Recorded – handling chemistry (no dosing) |
| nad+ 500 mg reconstitution | Handling + fill mass | Fill-mass label prepended to handling term | 500 mg lyophilised fill dissolved in a stated volume | Recorded – handling chemistry (no dosing) |
| nad 500 mg reconstitution | Handling + fill mass | Charge symbol dropped | Same referent as row above | Recorded – handling chemistry (no dosing) |
| how to reconstitute nad+ 500 mg | Procedural question | Question form of the handling term | Concentration = fill mass ÷ diluent volume | Recorded – handling chemistry; no protocol issued |
| how to reconstitute 500mg nad+ | Procedural question | Mass token moved before compound token | Same referent as row above | Recorded – handling chemistry; no protocol issued |
| reconstituting nad+ 500mg | Procedural gerund | Verb-form variant | Same referent as row above | Recorded – handling chemistry; no protocol issued |
| 500mg nad+ reconstitution | Handling + fill mass | Mass-first token order | Same referent as row above | Recorded – handling chemistry (no dosing) |
| nad+ 1000mg reconstitution | Handling + fill mass | 1,000 mg fill-mass variant | 1,000 mg lyophilised fill | Recorded – handling chemistry (no dosing) |
| lyophilized nad+ | State descriptor | Freeze-dried solid named explicitly | β-NAD+ lyophilisate | Recorded – handling terminology |
| nad500 | Fill-mass concatenation | Compound + mass fused without unit | 500 mg fill label | Recorded – fill-mass nomenclature |
| nad+500 | Fill-mass concatenation | Charge symbol retained, unit dropped | 500 mg fill label | Recorded – fill-mass nomenclature |
| nad + 500 mg | Fill-mass token | Spaces inserted around the charge symbol | 500 mg fill label | Recorded – fill-mass nomenclature |
| nad+500mg peptide | Fill mass + category error | Mass fused; 'peptide' appended by metonymy | 500 mg β-NAD+ fill (not a peptide) | Recorded – category corrected |
| nad 50mg | Fill-mass token | 50 mg fill | 50 mg fill label | Recorded – fill-mass nomenclature |
| nad 200 mg | Fill-mass token | 200 mg fill | 200 mg fill label | Recorded – fill-mass nomenclature |
| nad 750 mg | Fill-mass token | 750 mg fill | 750 mg fill label | Recorded – fill-mass nomenclature |
| nad+ 1000 mg | Fill-mass token | 1,000 mg fill | 1,000 mg fill label | Recorded – fill-mass nomenclature |
| 1000 mg nad | Fill-mass token | Mass-first order, charge dropped | 1,000 mg fill label | Recorded – fill-mass nomenclature |
| peptide nad+ | Category error | Catalogue-section metonymy: NAD+ listed beside peptides | β-NAD+ (dinucleotide) | Recorded – category corrected |
| peptide nad plus | Category error | 'plus' spelled out for the charge | β-NAD+ (dinucleotide) | Recorded – category corrected |
| nad plus peptides | Category error | Plural, 'plus' spelled out | β-NAD+ (dinucleotide) | Recorded – category corrected |
| nad and peptides | Co-listing query | Conjunction: NAD+ alongside peptide catalogues | β-NAD+ + peptide class (distinct chemistries) | Recorded – co-listing terminology |
| peptides and nad | Co-listing query | Reversed conjunction | Same referent as row above | Recorded – co-listing terminology |
| is nad plus a peptide | Category question | Direct classification question | No – see Section 2 | Recorded – category corrected |
| is nad + a peptide | Category question | Space inserted before charge | No – see Section 2 | Recorded – category corrected |
| nad peotide | Orthographic error | Vowel transposition (peptide → peotide) | β-NAD+ (dinucleotide) | Recorded – orthography + category corrected |
| nad+ research peptide | Category error + scope | 'Research' qualifier retained; 'peptide' erroneous | β-NAD+ research-grade reagent | Recorded – category corrected |
| nad+ bpc 157 peptide | Co-listing query | NAD+ juxtaposed with the gastric pentadecapeptide | Two unrelated reagents; no combination literature located | Recorded – co-listing; no blend evidence |
| 5 amino 1mq with nadh | Co-listing query | NNMT inhibitor juxtaposed with the reduced dinucleotide | 5-Amino-1MQ + NADH (mechanistically linked via NNMT/NAD+ salvage) | Recorded – co-listing; pathway note only |
| nad strips | Dosage-form descriptor | Orally dissolving film format named | Film dosage form (not characterised for NAD+ in the located literature) | Recorded – dosage-form terminology; no route guidance |
| nad+ strips | Dosage-form descriptor | Charge symbol retained | Same referent as row above | Recorded – dosage-form terminology; no route guidance |
| nad dissolvable strips | Dosage-form descriptor | 'dissolvable' qualifier | Same referent as row above | Recorded – dosage-form terminology; no route guidance |
| nad sublingual strips | Route-qualified dosage form | Administration route appended | Same format; route term declined | Declined – route/administration query |
| nad 500 mg injection | Route-qualified fill mass | Administration route appended | 500 mg fill; route term declined | Declined – route/administration query |
| nad+ 500mg injection | Route-qualified fill mass | Administration route appended | Same as row above | Declined – route/administration query |
| nad+ peptide for sale | Commercial query | Transactional modifier | β-NAD+ reagent listing | Declined – commercial intent; no vendor assessed |
| nad peptides for sale | Commercial query | Plural transactional variant | β-NAD+ reagent listing | Declined – commercial intent; no vendor assessed |
| buy nad+ peptide | Commercial query | Verb-first transactional variant | β-NAD+ reagent listing | Declined – commercial intent; no vendor assessed |
| peptide sciences nad | Vendor-anchored token | Catalogue brand token prepended | β-NAD+ reagent listing at a named vendor | Recorded – vendor token; no vendor assessed or endorsed |
| short chain aminos nad | Vendor-anchored token | Catalogue brand token prepended | β-NAD+ reagent listing at a named vendor | Recorded – vendor token; no vendor assessed or endorsed |
7. Related Research Reviews on Peptide Insider
NAD+ chemistry intersects several clusters already reviewed on this site. For readers navigating by topic:
- NAD+ and mitochondrial metabolism: NAD+ compound review · 5-Amino-1MQ and NNMT inhibition · NNMT inhibitor family nomenclature · MOTS-c · humanin · SS-31 (elamipretide) · metabolic-axis nomenclature review
- Handling and reconstitution chemistry: bacteriostatic water and reconstitution media · laboratory syringes and needles · BPC-157 stability and handling
- Catalogue formats and quality verification: catalogue formats and fill-mass vocabulary · vendor-independent quality verification · how to evaluate research peptide suppliers
- Query-orthography companions: FOXO4-DRI / melanotan / BPC-157 orthography crosswalk · BPC-157 compound review (for the co-listing token "nad+ bpc 157 peptide")
8. Where to Source for Research
Research-grade β-NAD+ in both free-acid and buffered lyophilised presentations is catalogued by several suppliers serving the research-use-only market, including Short Chain Aminos, BioPep, Catalyst Research and Apex Research Services. When comparing listings, the chemistry in Sections 2–4 suggests three questions worth putting to any certificate of analysis: whether the stated mass is free-acid equivalent or salt mass, whether identity and purity were confirmed by LC-MS or HPLC, and what counter-ion the buffered presentation contains. No supplier is assessed or endorsed here, and availability is noted for research reference only.
9. Frequently Asked Research Questions
What is buffered NAD+ and how does it differ from unbuffered NAD+?
Buffered NAD+ is β-nicotinamide adenine dinucleotide co-lyophilised with a base (sodium bicarbonate, or neutralised to the sodium salt) so that dissolution yields a near-neutral solution. Unbuffered NAD+ is the free acid, which dissolves to an acidic solution. The molecule is identical; the pH of the reconstituted solution and the counter-ion differ.
Is NAD+ a peptide?
No. NAD+ is a pyridine dinucleotide composed of nicotinamide, two ribose units, a pyrophosphate bridge and adenine. It contains no amino acid residues and no amide backbone. Catalogue tokens such as "peptide nad+" and "nad plus peptides" reflect vendor category placement, not chemistry.
Which presentation is more stable in solution, buffered or unbuffered NAD+?
The literature indicates that NAD+ is most stable in mildly acidic solution and is hydrolysed faster as pH rises, with buffer anions accelerating the reaction (Lowry 1961; Anderson & Anderson 1963). An unbuffered free-acid solution is therefore the more intrinsically stable stock, while a buffered solution offers pH compatibility with sensitive research systems.
What does "nad500" or "nad+ 1000 mg" mean on a catalogue label?
These are nominal lyophilised fill masses (500 mg or 1,000 mg of solid per vial). Fill mass is a label quantity; it is not a concentration and not a use instruction. For buffered presentations, confirm whether the figure is free-acid equivalent or salt mass.
Does this review provide a reconstitution protocol for NAD+ 500 mg?
No. It records the chemistry any protocol must respect (pH-dependent hydrolysis, buffer catalysis, diluent choice) but issues no procedures, quantities or administration guidance. All content is strictly for research reference; not for human or veterinary use.
Can NAD+ and NADH be handled under the same pH conditions?
Not optimally. NAD+ is acid-stable and alkali-labile, whereas NADH is alkali-stable and acid-labile (Lowry 1961; Burton & Kaplan 1963). The two redox states require opposite pH regimes for maximum stability.
Works Cited
- Cantó C, Menzies KJ, Auwerx J. NAD+ metabolism and the control of energy homeostasis: a balancing act between mitochondria and the nucleus. Cell Metab. 2015;22(1):31-53. PMID: 26118927. DOI: 10.1016/j.cmet.2015.05.023.
- Covarrubias AJ, Perrone R, Grozio A, Verdin E. NAD+ metabolism and its roles in cellular processes during ageing. Nat Rev Mol Cell Biol. 2021;22(2):119-141. PMID: 33353981. DOI: 10.1038/s41580-020-00313-x.
- Lowry OH, Passonneau JV, Rock MK. The stability of pyridine nucleotides. J Biol Chem. 1961;236:2756-2759. PMID: 14466980.
- Anderson BM, Anderson CD. The effect of buffers on nicotinamide adenine dinucleotide hydrolysis. J Biol Chem. 1963;238:1475-1478. PMID: 14012814.
- Burton RM, Kaplan NO. The reaction of reduced pyridine nucleotides with acid. Arch Biochem Biophys. 1963;101:150-159. PMID: 14017248. DOI: 10.1016/0003-9861(63)90545-9.
- Johnson SL, Tuazon PT. Acid-catalyzed hydration of reduced nicotinamide adenine dinucleotide and its analogues. Biochemistry. 1977;16(6):1175-1183. PMID: 14674. DOI: 10.1021/bi00625a023.
- Wu JT, Wu LH, Knight JA. Stability of NADPH: effect of various factors on the kinetics of degradation. Clin Chem. 1986;32(2):314-319. PMID: 3943190.
- Bernofsky C. Isolation and identification of 2'-phosphoadenosine diphosphate, an alkali-degradation product of nicotinamide adenine dinucleotide phosphate. Arch Biochem Biophys. 1975;166(2):485-493. PMID: 235242. DOI: 10.1016/0003-9861(75)90431-2.
- Chenault HK, Whitesides GM. Regeneration of nicotinamide cofactors for use in organic synthesis. Appl Biochem Biotechnol. 1987;14(2):147-197. PMID: 3304160. DOI: 10.1007/BF02798431.
- Manning MC, Chou DK, Murphy BM, Payne RW, Katayama DS. Stability of protein pharmaceuticals: an update. Pharm Res. 2010;27(4):544-575. PMID: 20143256. DOI: 10.1007/s11095-009-0045-6.
- Trammell SA, Brenner C. Targeted, LCMS-based metabolomics for quantitative measurement of NAD+ metabolites. Comput Struct Biotechnol J. 2013;4:e201301012. PMID: 24688693. DOI: 10.5936/csbj.201301012.
- Revollo JR, Grimm AA, Imai S. The NAD biosynthesis pathway mediated by nicotinamide phosphoribosyltransferase regulates Sir2 activity in mammalian cells. J Biol Chem. 2004;279(50):50754-50763. PMID: 15381699. DOI: 10.1074/jbc.M408388200.
- Nikiforov A, Dölle C, Niere M, Ziegler M. Pathways and subcellular compartmentation of NAD biosynthesis in human cells: from entry of extracellular precursors to mitochondrial NAD generation. J Biol Chem. 2011;286(24):21767-21778. PMID: 21504897. DOI: 10.1074/jbc.M110.213298.
- Camacho-Pereira J, Tarragó MG, Chini CCS, et al. CD38 dictates age-related NAD decline and mitochondrial dysfunction through an SIRT3-dependent mechanism. Cell Metab. 2016;23(6):1127-1139. PMID: 27304511. DOI: 10.1016/j.cmet.2016.05.006.
- Liu L, Su X, Quinn WJ 3rd, et al. Quantitative analysis of NAD synthesis-breakdown fluxes. Cell Metab. 2018;27(5):1067-1080.e5. PMID: 29685734. DOI: 10.1016/j.cmet.2018.03.018.
- Yoshino J, Baur JA, Imai SI. NAD+ intermediates: the biology and therapeutic potential of NMN and NR. Cell Metab. 2018;27(3):513-528. PMID: 29249689. DOI: 10.1016/j.cmet.2017.11.002.
- Rajman L, Chwalek K, Sinclair DA. Therapeutic potential of NAD-boosting molecules: the in vivo evidence. Cell Metab. 2018;27(3):529-547. PMID: 29514064. DOI: 10.1016/j.cmet.2018.02.011.
- Ratajczak J, Joffraud M, Trammell SA, et al. NRK1 controls nicotinamide mononucleotide and nicotinamide riboside metabolism in mammalian cells. Nat Commun. 2016;7:13103. PMID: 27725675. DOI: 10.1038/ncomms13103.
- Grozio A, Mills KF, Yoshino J, et al. Slc12a8 is a nicotinamide mononucleotide transporter. Nat Metab. 2019;1(1):47-57. PMID: 31131364. DOI: 10.1038/s42255-018-0009-4.
- Airhart SE, Shireman LM, Risler LJ, et al. An open-label, non-randomized study of the pharmacokinetics of the nutritional supplement nicotinamide riboside (NR) and its effects on blood NAD+ levels in healthy volunteers. PLoS One. 2017;12(12):e0186459. PMID: 29211728. DOI: 10.1371/journal.pone.0186459.
- Clement J, Wong M, Poljak A, Sachdev P, Braidy N. The plasma NAD+ metabolome is dysregulated in "normal" aging. Rejuvenation Res. 2019;22(2):121-130. PMID: 30124109. DOI: 10.1089/rej.2018.2077.
Research-use-only disclaimer. This article is a literature review prepared for research reference. It does not describe, recommend or imply any use of NAD+ or any other compound in humans or animals; it contains no dosing, reconstitution-protocol or administration guidance; and it makes no health, therapeutic or cosmetic claims. All content is strictly for research reference; not for human or veterinary use.