| Field | Specification |
|---|---|
| Activity | |
| Alternative Names | Malonyl-CoA |
| Form | Lyophilized powder |
| Molecular Weight | |
| Product Type | |
| Purity | |
| Shipping | |
| SMILES | |
| Solubility | Soluble in water |
| Storage |
Overview
Malonyl Coenzyme A, Free Acid 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: Malonyl-CoA.
Key Elements and Design Rationale
- Formula / MW / Purity: C24H38N7O19P3S; 853.58 g/mol; ≥ 95%. The Free Acid form provides enhanced aqueous stability.
- Form / Solubility: Lyophilized powder; Soluble in water.
- Synonyms: Malonyl-CoA.
- Origin: Biosynthetic synthesis.
Biological Background
Malonyl Coenzyme A (Malonyl-CoA) is a coenzyme A derivative formed by the carboxylation of acetyl-CoA, playing a key role in fatty acid and polyketide synthesis, as well as the transport of ?-ketoglutarate across the mitochondrial membrane. It regulates metabolic processes by inhibiting carnitine palmitoyltransferase 1, affecting fatty acid transfer into mitochondria. High levels of malonyl CoA have been associated with cellular processes like cancer cell apoptosis (Pate, 2014; Cadenas et al., 2016).
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
To quote quickly, tell us: compound name + CAS/structure (SMILES or mol file), intended assay context, solvent preference, salt/stereochemistry requirements, purity/QC level, and the amount (mg–g).
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Send the CAS or structure and your specs. We can help source it, suggest close
equivalents, or discuss custom synthesis with the right QC documentation (RUO).
Pate, R. (2014). Malonyl-CoA and cancer cell metabolism. Journal of Cellular Biochemistry, 115(2), 227–233.
Cadenas, E., Arduini, A., & Sarti, P. (2016). Malonyl-CoA in metabolic regulation: Implications for cell survival and cancer. Cell Death & Disease, 7(1), e1089.
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