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| Product Name | Coenzyme A (CoA, Trilithium Salt) |
| Catalog No. | IEC-HMM-0064 |
| Description | Coenzyme A in its reduced form (CoASH), supplied as trilithium salt. CoA is the universal acyl group carrier in metabolism, participating in the synthesis and oxidation of fatty acids, the tricarboxylic acid (TCA) cycle via acetyl-CoA, and numerous enzymatic acyl-transfer reactions central to cellular energy metabolism. |
| Intended Use | Cofactor for acetyltransferase and acyltransferase enzyme assays; substrate for citrate synthase, acetyl-CoA synthetase, and carnitine acetyltransferase reactions; component in coupled enzyme systems for clinical metabolite quantification; biochemical research into fatty acid metabolism and the TCA cycle. |
| Principle / Technology | CoA functions through its terminal thiol (-SH) group, which forms high-energy thioester bonds with acyl groups (e.g., acetyl-CoA). The thioester bond has a high standard free energy of hydrolysis (ΔG°' ~ -31.5 kJ/mol for acetyl-CoA), enabling acyl group transfer in biosynthetic and energy-yielding metabolic pathways. |
| Detection Method | Purity analyzed by HPLC. Thiol content determined by DTNB (Ellman's reagent) assay. Enzymatic activity verified using phosphate acetyltransferase or citrate synthase coupled assays. |
| Sample Type | Substrate solution for CoA-dependent enzyme assays. |
| Performance Range / Specifications | Purity >= 95% by HPLC. Free thiol content >= 90% of theoretical. Working concentration: 0.05-0.5 mM in most enzyme assays. |
| Sensitivity / LOD | Enables detection of CoA at concentrations as low as 1 uM by DTNB assay, or sub-uM with enzymatic cycling methods. |
| Specificity | Specifically recognized by CoA-dependent enzymes. Oxidized CoA (CoA disulfide) does not function as an acyl acceptor and must be reduced prior to use in thiol-dependent reactions. |
| Reaction Conditions / Protocol | For acetyltransferase assays: 0.1-0.5 mM CoA in appropriate buffer with acetyl donor, enzyme, and detection system. Monitor thioester bond formation at 232 nm (ε ~ 4,500 M⁻¹cm⁻¹) or couple to DTNB for thiol consumption at 412 nm. |
| Components / Formulation | Coenzyme A, trilithium salt. Supplied as lyophilized powder or custom-configured solution. |
| Storage Conditions | Lyophilized: store at -20 °C, desiccated. Solution: -20 °C to -80 °C in single-use aliquots under inert gas to prevent oxidation. |
| Shelf Life | Lyophilized: 36 months at -20 °C (desiccated). Reconstituted: prepare fresh or aliquot and store at -80 °C for up to 3 months. |
| Package Specifications | 10 mg, 50 mg, 100 mg, 500 mg, 1 g. Bulk packaging available for industrial applications. |
| Product Form | White to off-white lyophilized powder. Hygroscopic and air-sensitive (free thiol). |
| Quality Control | HPLC purity; DTNB thiol assay; enzymatic activity with phosphate acetyltransferase; moisture content; lithium and heavy metal analysis; absence of CoA disulfide degradation product by HPLC. |
| Key Features | Central cofactor in cellular energy metabolism; reactive free thiol for thioester bond formation; high-purity lithium salt for controlled counterion composition; applicable to both endpoint and kinetic enzyme assay formats. |
| Purity | >= 95% by HPLC. Free thiol >= 90%. |
| Concentration | Lyophilized powder. Typical reconstitution: 10-50 mM in deoxygenated buffer. |
| Activity / Unit Definition | Functional in all standard CoA-dependent enzyme systems. Activity verified using phosphate acetyltransferase with acetyl phosphate as acetyl donor. |
| Molecular Weight | 785.5 g/mol (trilithium salt, free acid equivalent ~767.5 g/mol). |
| Source / Origin | Produced via fermentation using engineered microorganisms (bacteria or yeast) followed by multi-step chromatographic purification. Alternatively synthesized from pantothenic acid, cysteine, and ATP by enzymatic conversion. |
| pH Range / Optimal pH | Stable at pH 2.0-6.0 (minimal thiol oxidation). Working pH for enzyme assays: 7.0-8.5. Thiol reactivity increases at alkaline pH but stability decreases. |
| Shipping Conditions | Lyophilized: ambient temperature. Reconstituted solution: ship on dry ice. |
| Expiration Date / Stability | 36 months (lyophilized, desiccated, -20 °C). Reconstituted: free thiol content decreases ~5-10% per month at -80 °C; use promptly for quantitative applications. |
| Regulatory / Compliance | ISO 9001 certified. For research and IVD reagent formulation. Not intended for direct human administration. |
| Compatibility | Substrate for all CoA-dependent transferases and ligases. Compatible with common biochemical buffers (Tris, phosphate, HEPES) containing 1-5 mM EDTA or EGTA. DTT (1 mM) helps maintain reduced thiol state during long incubations. |
| Recommended Buffer System | Reconstitute in deoxygenated 10 mM sodium acetate (pH 5.0-6.0) for maximum thiol stability. Dilute into assay buffer at time of use. |
| Application Notes / Precautions | Handle under inert gas (nitrogen or argon) for critical quantitative work. Prepare solutions fresh daily. Monitor thiol content with DTNB if solutions are stored. The free thiol of CoA is essential for activity; oxidized CoA must be reduced with DTT or TCEP before use. |
| Batch-to-Batch Consistency | HPLC purity and free thiol content verified per batch. Enzymatic activity within +/- 10% of reference standard. |
For research use only, not for clinical use.
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