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Peptide Bundles

Redox Research Pair

$104.99

The Redox Research Pair supplies NAD+ at 500 mg and glutathione at 600 mg. Both are described as redox compounds, but they occupy different roles: glutathione is a thiol redox buffer and a direct antioxidant, while NAD+ is a redox cofactor carrying electrons in catabolic metabolism. The two connect indirectly, through NADP+ and NADPH. Supplied lyophilized. For research use only.

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Redox Research Pair
Product Profile

Overview

The Redox Research Pair brings together the two compounds most often grouped under cellular redox research, and the pairing is more useful once their roles are separated.

Glutathione is a tripeptide and the cell’s principal low-molecular-weight thiol. The ratio between its reduced form, GSH, and its oxidised dimer, GSSG, is a standard readout of cellular oxidative state, and glutathione performs antioxidant work directly through the free thiol on its cysteine residue.

NAD+ is a dinucleotide coenzyme rather than a peptide, and it is not an antioxidant. It carries electrons in catabolic metabolism, cycling between NAD+ and NADH, and the NAD+/NADH ratio reflects metabolic flux rather than oxidative stress. The two ratios therefore measure different variables.

The compounds do connect, indirectly. Glutathione reductase regenerates GSH from GSSG using NADPH — not NADH — and NADP+ is produced from NAD+ by NAD kinase. The route runs through three enzymatic steps and a separate pyridine nucleotide pool.

Glutathione is also an unusual peptide: its glutamate is joined through a gamma peptide bond rather than a standard backbone linkage, which is why no ribosome assembles it. Both compounds are supplied lyophilized with batch documentation.

For Research Use Only. Not intended for human consumption, therapeutic use, veterinary use, or diagnostic applications.

The Redox Research Pair is a two-vial set containing NAD+ at 500 mg and glutathione at 600 mg. Glutathione is a thiol redox buffer and a direct antioxidant; NAD+ is a redox cofactor that carries electrons in metabolism and is not an antioxidant. The two connect indirectly, through NADP+ and NADPH rather than directly.

Key Takeaways

  • The Redox Research Pair contains one NAD+ vial at 500 mg and one glutathione vial at 600 mg, supplied lyophilized.
  • Glutathione is a thiol redox buffer, and the GSH to GSSG ratio is a standard readout of cellular oxidative state.
  • NAD+ is a redox cofactor rather than an antioxidant; the NAD+ to NADH ratio reflects metabolic flux, not oxidative stress.
  • The two systems connect through three enzymatic steps: NAD+ to NADP+, NADP+ to NADPH, and NADPH used by glutathione reductase.
  • Glutathione is a tripeptide joined through a gamma peptide bond and is assembled enzymatically rather than by ribosomes; NAD+ is not a peptide at all.
  • Both compounds are supplied strictly for laboratory research and are not intended for human consumption, therapeutic use, veterinary use, or diagnostic applications.

What’s Included in This Research Pair

CompoundMassMolecular classRedox roleWhy it is included
NAD+500 mgDinucleotide coenzymeElectron carrier in catabolic metabolismRepresents the metabolic redox couple, NAD+/NADH
Glutathione600 mgTripeptide, gamma-linkedThiol redox buffer and direct antioxidantRepresents the oxidative-state redox couple, GSH/GSSG

Both are supplied as lyophilized material with batch documentation. On a molar basis the two masses are broadly comparable — roughly 750 µmol of NAD+ against roughly 1,950 µmol of glutathione — though salt form affects both figures.

“Redox” Means Two Different Things Here

Both compounds are routinely described as redox compounds. The word applies to each in a different sense, and the difference determines what an experiment using them can conclude.

Glutathione is a redox buffer

Glutathione is the principal low-molecular-weight thiol in most cells. Its cysteine residue carries a free thiol group, which is the reactive site. Two glutathione molecules can oxidise to form the disulfide dimer GSSG, and glutathione reductase converts GSSG back to reduced glutathione.

The ratio between reduced and oxidised glutathione is itself a widely used measure of cellular oxidative state. Glutathione performs antioxidant work directly, acting as a substrate for glutathione peroxidases and participating in conjugation reactions through glutathione S-transferases.

NAD+ is a redox cofactor, not an antioxidant

NAD+ does not scavenge reactive species and does not reduce oxidised protein thiols. It is an electron carrier: catabolic dehydrogenases reduce NAD+ to NADH, and NADH delivers electrons into the electron transport chain.

NAD+ is separately consumed — not cycled — as a substrate by enzyme families including sirtuins and PARPs, which cleave it rather than reducing it. Neither role is antioxidant activity.

Vendor descriptions frequently present NAD+ as an antioxidant. That characterisation is incorrect, and a study built on it will attribute an observation to the wrong mechanism.

The two ratios measure different variables

The GSH/GSSG ratio is a measure of oxidative state. The NAD+/NADH ratio is a measure of metabolic flux and energy state.

A researcher measuring one is not measuring the other, and the two can move independently. Grouping both under “redox” as though they were interchangeable readouts of a single variable produces experiments that do not measure what they report.

Why hold bothNot because the compounds act together, but because separating their contributions requires having both. Any glutathione response attributed to NAD+ availability passes through three independently regulated enzymatic steps — see the route below.
Aviso de InvestigaciónTodos los productos de cada categoría son únicamente para uso en investigación y no aptos para uso humano o veterinario, diagnóstico o tratamiento.
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READ

(preguntas frecuentes)

Preguntas Frecuentes

01

What is included in the Redox Research Pair?

The pair includes one NAD+ vial at 500 mg and one glutathione vial at 600 mg, both supplied lyophilized with batch documentation. The two compounds represent different redox roles — a metabolic electron carrier and a thiol redox buffer. For research use only.
02

Is NAD+ an antioxidant?

No. NAD+ is a redox cofactor that carries electrons in catabolic metabolism. It does not scavenge reactive species or reduce oxidised protein thiols. It is also consumed as a substrate by sirtuins and PARPs. Neither role constitutes antioxidant activity, despite frequent vendor claims otherwise.
03

Can NAD+ and glutathione be studied together?

Yes, and the pairing has a specific rationale. The two systems connect through three enzymatic steps: NAD+ to NADP+, NADP+ to NADPH, and NADPH used by glutathione reductase to regenerate reduced glutathione. Separating contributions along that route requires having both compounds available.
04

How are NAD+ and glutathione connected?

Indirectly, through NADPH. Glutathione reductase regenerates reduced glutathione using NADPH rather than NADH, and NADP+ is produced from NAD+ by NAD kinase. The route runs NAD+ to NADP+ to NADPH to glutathione regeneration — three enzymatic steps through a separate nucleotide pool.
05

What is the difference between the GSH/GSSG ratio and the NAD+/NADH ratio?

They measure different variables. The GSH/GSSG ratio indicates cellular oxidative state. The NAD+/NADH ratio indicates metabolic flux and energy state. The two can move independently, and treating them as interchangeable readouts of one variable is a common source of misinterpretation.
06

Is glutathione a peptide?

Yes, but an unusual one. Glutathione is a tripeptide of glutamate, cysteine and glycine, with its glutamate joined through a gamma peptide bond formed from the side-chain carboxyl rather than the backbone. That linkage is why no ribosome assembles glutathione.
07

Why is glutathione not made by ribosomes?

Ribosomal synthesis produces alpha peptide bonds only. Glutathione's gamma-glutamyl linkage cannot be formed that way, so it is assembled instead by two ATP-dependent enzymes — glutamate-cysteine ligase and glutathione synthetase — acting in sequence.
08

Should I order reduced or oxidised glutathione?

Reduced glutathione, GSH, carries the free thiol that performs the functional work; the oxidised dimer GSSG does not. A purity figure alone does not establish which form predominates, so confirm that the certificate of analysis specifies reduced glutathione content rather than total glutathione.
09

Does a glutathione certificate of analysis show GSH or GSSG?

It depends on the supplier, and this is worth confirming before ordering. Some certificates report total glutathione or overall purity without distinguishing the reduced and oxidised forms. A batch that has partially oxidised can report high purity while containing a substantial GSSG fraction.
10

Is NAD+ a peptide?

No. NAD+ is a dinucleotide coenzyme, consisting of two nucleotides joined through a pyrophosphate bridge. It contains no amino acids and no peptide bonds, and it should be specified and handled as a coenzyme rather than by peptide criteria.
11

Do the two compounds need different storage?

Both are stored lyophilized at reduced temperature, but their degradation routes differ. Glutathione is vulnerable to thiol oxidation, which converts it to GSSG on air exposure. NAD+ is separately subject to pyrophosphate hydrolysis. Equivalent storage conditions do not imply equivalent stability.
12

Does supplying NAD+ raise glutathione levels?

Not directly, and the question is harder than it appears. Any such effect would pass through NAD kinase, the pentose phosphate pathway and glutathione reductase, each independently regulated. An effect observed at the glutathione end may originate at any of those steps rather than from NAD+ supply itself.
13

Have these two compounds been studied together as supplied materials?

No published study has examined them together as co-supplied research materials. The biochemical relationship between the systems is well characterised in the literature, but that is different from a controlled study of the two as a research pairing.
14

Can these compounds be used on humans or animals?

No. Both vials are supplied for laboratory research only. They are not intended for human consumption, therapeutic use, veterinary use, or diagnostic applications, and no dosing, protocol or administration guidance is provided for them.