| Field | Specification |
|---|---|
| Activity | |
| Alternative Names | CoA–S-S–CoA, CoA disulfide |
| Form | Lyophilized powder |
| Molecular Weight | |
| Product Type | |
| Purity | |
| Shipping | |
| SMILES | |
| Solubility | Soluble in water |
| Storage |
Overview
Coenzyme A oxidized, Sodium salt is a biochemical supplied by Coenza for use in enzymology and metabolic research. Available as Lyophilized powder, purity ≥ 95%, suitable for in vitro assays and pathway studies.
Also known as: CoA–S-S–CoA, CoA disulfide.
Key Elements and Design Rationale
- Formula / MW / Purity: C42H64N14O32P6S2 · xNa; 1533.05 g/mol (free acid basis); ≥ 95%. The Sodium salt form provides enhanced aqueous stability.
- Form / Solubility: Lyophilized powder; Soluble in water.
- Synonyms: CoA–S-S–CoA, CoA disulfide.
- Origin: Biosynthetic synthesis.
Biological Background
Coenzyme A (CoA) is an essential cofactor found in all living organisms, playing a crucial role in various biochemical processes. It is synthesized through the enzymatic conjugation of cysteine, pantothenate (Vitamin B5), and adenosine triphosphate (ATP). Oxidized CoA is commonly used to investigate CoA disulfide reductase (CoADR) systems, which regenerate reduced CoA in vivo, and to explore its distinct biological roles within cellular systems (Liu et al., 2016; Wu et al., 2012).
Research Relevance and Current Trends
- Acyl-CoA metabolism increasingly linked to histone acylation marks and epigenetic regulation in cancer and metabolic disease research.
- Growing interest in short-chain fatty acid CoA thioesters as mediators of gut microbiome–host metabolic crosstalk.
- CoA-dependent enzymes investigated as drug targets in infectious disease and neurometabolic disorder research.
Common Research Applications
- Enzyme kinetics assays — direct substrate for acyltransferases, thiolases, and dehydrogenases.
- Metabolic flux analysis — isotope-labeled variants available for stable-isotope tracing.
- In vitro pathway reconstitution for fatty acid β-oxidation, TCA cycle, or polyketide biosynthesis.
- Biochemical characterization of CoA-binding proteins by activity assays or binding measurements.
Notes for Experimental Interpretation
- CoA thioesters hydrolyze at neutral–alkaline pH; prepare working solutions fresh and keep on ice.
- Different salt forms share the same core structure — normalize concentrations using the free-acid MW when comparing across forms.
- Thiol oxidation may occur upon air exposure; use under inert atmosphere or with reducing agents where appropriate.
Need this compound in a format that drops straight into your assay? We can tailor formulation, chemistry, and documentation so your results stay consistent across runs and re-orders.
- Format options: solid or pre-dissolved solution (choose solvent), target concentration, aliquots, light/moisture-protected packaging
- Chemistry options: free base/acid vs salt forms, hydrate/solvate preference, stereoisomer control (single enantiomer or racemate), close analogs
- Add-on labels & handles: D/¹³C/¹⁵N isotopes (LC-MS/internal standards), azide/alkyne or other functional handles for conjugation
- QC & documentation: standard COA or enhanced analytical pack (HPLC/LC-MS/NMR), chiral purity, residual solvents, water content (KF), method-specific specs
- Scale & continuity: mg to gram scale, bulk pricing, lot reservation, repeat-order continuity
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equivalents, or discuss custom synthesis with the right QC documentation (RUO).
Liu, S., Wang, T., & Zhang, D. (2016). Coenzyme A disulfide reductase: Insights into the role of CoADR in coenzyme A metabolism. Journal of Biological Chemistry, 291(43), 22568–22575.
Wu, Y., Shi, W., & Liu, Q. (2012). Mechanistic studies of CoA disulfide reductase systems in cellular redox regulation. Free Radical Biology & Medicine, 53(4), 644–651.
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