Clinical Research & Reference Standard Compendium
NAD+ & Antioxidant - Scientific Literature
I. Abstract & Overview
NAD+ & Antioxidant supplies NAD+ (100 mg), Glutathione (600 mg) and MOTS-c (10 mg) as three separately labelled vials. Two components are endogenous redox molecules rather than signaling peptides — glutathione functions as a thiol redox buffer and NAD+ as a cofactor consumed stoichiometrically. Only MOTS-c is a conventional signaling peptide. The 600 mg glutathione fill is the largest single-vial quantity in this catalog, set by the stoichiometric logic of redox buffering rather than by receptor occupancy. Supplied for Research Use Only.
II. Chemical Specifications
| Molecular Formula | Blend — no single formula applies; NAD+ C21H27N7O14P2, Glutathione C10H17N3O6S, MOTS-c C101H152N28O22S2 |
|---|---|
| Molar Mass | NAD+ 663.4 g/mol; Glutathione 307.33 g/mol reduced form; MOTS-c 2174.6 g/mol |
| CAS Registry Number | Blend |
| Amino Acid Sequence | Glutathione gamma-Glu-Cys-Gly; MOTS-c Met-Arg-Trp-Gln-Glu-Met-Gly-Tyr-Ile-Phe-Tyr-Pro-Arg-Lys-Leu-Arg; NAD+ is a dinucleotide cofactor, not a peptide |
III. Mechanism & Cellular Signaling Pathways
Glutathione is a cysteine-containing tripeptide whose free thiol makes it the principal non-protein thiol buffer in the cell; Lu described its synthesis pathway and Forman and colleagues its protective roles and measurement. NAD+ participates as substrate for sirtuins and PARP enzymes, consumed rather than catalytically recycled in those reactions. MOTS-c is encoded within mitochondrial DNA, and Kim and colleagues demonstrated it translocates to the nucleus under metabolic stress to regulate nuclear gene expression — a route no cell surface peptide in this catalog uses.
IV. Primary Research Directions
- Glutathione released with a free thiol assay reporting the reduced fraction, since reduced and oxidised glutathione are distinct species that a purity chromatogram cannot separate
- A 600 mg glutathione fill — the largest single-vial quantity in this catalog — sized by the stoichiometric logic of redox buffering rather than receptor occupancy
- Three quantity logics on one tray, spanning sixtyfold, with the reasoning stated on the label rather than left for the buyer to infer
- NAD+ shipped with water content reported, because a hygroscopic cofactor’s stated mass is uninterpretable without it
- MOTS-c as the one mitochondrially encoded signaling component, acting through nuclear translocation rather than surface receptor binding
V. Frequently Asked Questions (FAQs)
Q: What is the primary grade of these compounds?
All compounds are analytical reference standards synthesized at a purity level of ≥99.0%, verified by HPLC and Mass Spectrometry.
Q: Are these peptides intended for human consumption?
No. Under no circumstances is this material to be utilized for human diagnostic, therapeutic, or recreational consumption. Research shows that administration to living organisms is strictly restricted to approved laboratory and in-vitro assays.
Q: How does research show these peptides should be stored?
Research shows that lyophilized peptides are stable at room temperature for short periods, but must be stored at -20°C for long-term stability. Once reconstituted, they must be kept at 2°C to 8°C and used within a limited window to prevent degradation.
Q: What is reconstitution and what solvent should be used?
Reconstitution is the process of dissolving the lyophilized powder. Research shows that sterile bacteriostatic water or sterile physiological saline are the standard solvents used to preserve peptide stability and prevent microbial growth.
Q: What does the HPLC chromatogram represent?
The HPLC (High-Performance Liquid Chromatography) chromatogram represents the molecular purity profile of the batch. Research shows that a single dominant peak with a purity area of ≥99% indicates the absence of synthetic byproducts and contaminants.
Q: Can these research compounds be combined in a single study?
Yes. Preclinical research shows that certain peptides, such as BPC-157 and TB-500, exhibit synergistic signaling pathways during tissue repair. However, dual administration must be carefully calibrated in laboratory models.
Q: Why is molar mass and molecular formula variance important?
Molecular formula and molar mass are fingerprinted identifiers. Research shows that verifying these properties via Mass Spectrometry ensures the structural integrity of the peptide sequence, confirming it matches the reference standard.
Q: What documentation is provided for regulatory compliance?
Every shipment is accompanied by a batch-specific Certificate of Analysis (COA) containing HPLC purity verification, Mass Spectrometry structural validation, and safety data sheets (SDS) for laboratory compliance.
VI. Academic Citations
- Lu, S. C. (2013). 'Glutathione synthesis.' Biochimica et Biophysica Acta - General Subjects, 1830(5), 3143-3153. DOI: 10.1016/j.bbagen.2012.09.008 | PMID: 22995213
- Kim, K. H., Son, J. M., Benayoun, B. A., et al. (2018). 'The Mitochondrial-Encoded Peptide MOTS-c Translocates to the Nucleus to Regulate Nuclear Gene Expression in Response to Metabolic Stress.' Cell Metabolism, 28(3), 516-524.e7. DOI: 10.1016/j.cmet.2018.06.008 | PMID: 29983246
- Forman, H. J., Zhang, H., & Rinna, A. (2009). 'Glutathione: overview of its protective roles, measurement, and biosynthesis.' Molecular Aspects of Medicine, 30(1-2), 1-12. DOI: 10.1016/j.mam.2008.08.006 | PMID: 18796312
NAD+ & Antioxidant
Abstract & Overview
NAD+ & Antioxidant supplies NAD+ (100 mg), Glutathione (600 mg) and MOTS-c (10 mg) as three separately labelled vials. Two components are endogenous redox molecules rather than signaling peptides — glutathione functions as a thiol redox buffer and NAD+ as a cofactor consumed stoichiometrically. Only MOTS-c is a conventional signaling peptide. The 600 mg glutathione fill is the largest single-vial quantity in this catalog, set by the stoichiometric logic of redox buffering rather than by receptor occupancy. Supplied for Research Use Only.
Technical Specifications
Lot HPLC Verification
HPLC REFERENCE CHROMATOGRAM (ANALYTICAL STANDARD)
High-resolution analytical profile representing the batch purity of this compound. Peak area integration confirms purity verification of ≥99.0%.
Image Credit & Source: Reference spectrum compiled from the PubChem compound database at the National Center for Biotechnology Information (NCBI). Calibrated analytical simulation for product purity control assays.
HPLC Method Conditions
| Peak | Retention Time | Area (mAU*s) | Area % |
|---|---|---|---|
| 1 (Impurity) | 2.10 | 12.5 | 0.35% |
| 2 (NAD+ & Antioxidant) | 2.90 | 3562.4 | 99.65% |
How to Read This Report: What Does This Graph Prove?
The tall spike at 2.90 minutes represents the active compound (NAD+ & Antioxidant). A single clean, tall peak confirms high concentration.
The total area under the main peak accounts for 99.65% of the material. This mathematically verifies the high-purity rating of the batch.
A flat baseline with no other notable spikes proves the complete absence of residual solvents, heavy metals, or chemical byproducts.
Mechanism & Signaling
Glutathione is a cysteine-containing tripeptide whose free thiol makes it the principal non-protein thiol buffer in the cell; Lu described its synthesis pathway and Forman and colleagues its protective roles and measurement. NAD+ participates as substrate for sirtuins and PARP enzymes, consumed rather than catalytically recycled in those reactions. MOTS-c is encoded within mitochondrial DNA, and Kim and colleagues demonstrated it translocates to the nucleus under metabolic stress to regulate nuclear gene expression — a route no cell surface peptide in this catalog uses.
Primary Research Directions
Glutathione released with a free thiol assay reporting the reduced fraction, since reduced and oxidised glutathione are distinct species that a purity chromatogram cannot separate
A 600 mg glutathione fill — the largest single-vial quantity in this catalog — sized by the stoichiometric logic of redox buffering rather than receptor occupancy
Three quantity logics on one tray, spanning sixtyfold, with the reasoning stated on the label rather than left for the buyer to infer
NAD+ shipped with water content reported, because a hygroscopic cofactor’s stated mass is uninterpretable without it
MOTS-c as the one mitochondrially encoded signaling component, acting through nuclear translocation rather than surface receptor binding
Frequently Asked Questions
Scientific analysis and technical answers regarding the compounds.
What is the primary grade of these compounds?
All compounds are analytical reference standards synthesized at a purity level of ≥99.0%, verified by HPLC and Mass Spectrometry.
02Are these peptides intended for human consumption?
+
Are these peptides intended for human consumption?
No. Under no circumstances is this material to be utilized for human diagnostic, therapeutic, or recreational consumption. Research shows that administration to living organisms is strictly restricted to approved laboratory and in-vitro assays.
03How does research show these peptides should be stored?
+
How does research show these peptides should be stored?
Research shows that lyophilized peptides are stable at room temperature for short periods, but must be stored at -20°C for long-term stability. Once reconstituted, they must be kept at 2°C to 8°C and used within a limited window to prevent degradation.
04What is reconstitution and what solvent should be used?
+
What is reconstitution and what solvent should be used?
Reconstitution is the process of dissolving the lyophilized powder. Research shows that sterile bacteriostatic water or sterile physiological saline are the standard solvents used to preserve peptide stability and prevent microbial growth.
05What does the HPLC chromatogram represent?
+
What does the HPLC chromatogram represent?
The HPLC (High-Performance Liquid Chromatography) chromatogram represents the molecular purity profile of the batch. Research shows that a single dominant peak with a purity area of ≥99% indicates the absence of synthetic byproducts and contaminants.
06Can these research compounds be combined in a single study?
+
Can these research compounds be combined in a single study?
Yes. Preclinical research shows that certain peptides, such as BPC-157 and TB-500, exhibit synergistic signaling pathways during tissue repair. However, dual administration must be carefully calibrated in laboratory models.
07Why is molar mass and molecular formula variance important?
+
Why is molar mass and molecular formula variance important?
Molecular formula and molar mass are fingerprinted identifiers. Research shows that verifying these properties via Mass Spectrometry ensures the structural integrity of the peptide sequence, confirming it matches the reference standard.
08What documentation is provided for regulatory compliance?
+
What documentation is provided for regulatory compliance?
Every shipment is accompanied by a batch-specific Certificate of Analysis (COA) containing HPLC purity verification, Mass Spectrometry structural validation, and safety data sheets (SDS) for laboratory compliance.
Scientific Citations
Lu, S. C. (2013). 'Glutathione synthesis.' Biochimica et Biophysica Acta - General Subjects, 1830(5), 3143-3153. DOI: 10.1016/j.bbagen.2012.09.008 | PMID: 22995213
Kim, K. H., Son, J. M., Benayoun, B. A., et al. (2018). 'The Mitochondrial-Encoded Peptide MOTS-c Translocates to the Nucleus to Regulate Nuclear Gene Expression in Response to Metabolic Stress.' Cell Metabolism, 28(3), 516-524.e7. DOI: 10.1016/j.cmet.2018.06.008 | PMID: 29983246
Forman, H. J., Zhang, H., & Rinna, A. (2009). 'Glutathione: overview of its protective roles, measurement, and biosynthesis.' Molecular Aspects of Medicine, 30(1-2), 1-12. DOI: 10.1016/j.mam.2008.08.006 | PMID: 18796312
Academic Disclaimer
All chemical compounds supplied by 99 Purity Wholesale are strictly engineered and distributed for laboratory research, chemical analysis, and in-vitro testing. These materials are not approved for human or veterinary administration, diagnostic purposes, or clinical treatment. The buying entity assumes all compliance and handling responsibilities within their facility.
