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Redox cofactors are the molecules that carry reducing equivalents through cellular metabolism, and they double as substrates for entire enzyme families. Pyridine dinucleotides serve NAD-dependent oxidoreductases as well as sirtuins and PARPs; thiol-based buffers set the intracellular redox potential and act as substrates for glutathione-S-transferases.
They are grouped by the chemistry they take part in, not by structure.
Laboratory research use only. Not for human or veterinary use.
What separates each of these from the others in the class.
Not a peptide at all — a small-molecule quinolinium. The choice when the target is the NNMT enzyme itself rather than a receptor or pathway.
Certificate of analysis →The buffer side — a tripeptide thiol that sets intracellular redox potential and serves as a glutathione-S-transferase substrate.
Certificate of analysis →The substrate side of redox biochemistry — a dinucleotide coenzyme for sirtuins, PARPs and NAD-dependent oxidoreductases.
Certificate of analysis →Handling: reconstitution storage and stability checking a certificate is genuine


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