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| Product Name | NADH (Reduced Nicotinamide Adenine Dinucleotide, Disodium Salt) |
| Catalog No. | IEC-HMM-0063 |
| Description | High-purity reduced beta-nicotinamide adenine dinucleotide (NADH) supplied as a disodium salt. NADH serves as a critical coenzyme in numerous oxidoreductase reactions, acting as an electron donor. It is a key component in coupled enzyme assays for clinical chemistry, metabolite quantification, and cell-based metabolic activity measurements. |
| Intended Use | Cofactor for dehydrogenase-based enzyme assays including lactate dehydrogenase, malate dehydrogenase, alcohol dehydrogenase, and glutamate dehydrogenase reactions. Used in clinical chemistry reagent formulations, coupled enzyme cycling assays for high-sensitivity metabolite detection, and cell metabolism analysis. |
| Principle / Technology | NADH functions as a two-electron carrier, donating a hydride ion (H⁻) to substrate in NADH-dependent dehydrogenase reactions, becoming oxidized to NAD⁺. The oxidation of NADH is accompanied by a decrease in absorbance at 340 nm (ε = 6,220 M⁻¹cm⁻¹), enabling direct spectrophotometric monitoring of enzymatic reactions. |
| Detection Method | Purity by HPLC and enzymatic cycling assay. Concentration by UV absorbance at 340 nm. Specific enzyme assay validation using lactate dehydrogenase standard. |
| Sample Type | Reagent component for NADH-dependent enzymatic assays. |
| Performance Range / Specifications | Purity >= 98% by HPLC; >= 95% enzymatic purity. NADH concentration verified spectrophotometrically. Suitable for assays requiring detection limits down to 0.1 uM NADH. |
| Sensitivity / LOD | Enables detection of enzyme activities down to 0.1 mU/mL in optimized coupled assay systems. |
| Specificity | Specifically utilized by NADH-dependent dehydrogenases. Not utilized by NADPH-dependent enzymes without appropriate transhydrogenase coupling. |
| Reaction Conditions / Protocol | Typically used at 0.1-0.3 mM final concentration in dehydrogenase assays. For substrate quantification by endpoint assay: 0.2-1 mM NADH. Prepare fresh solutions in appropriate buffer. |
| Components / Formulation | beta-NADH, reduced form, disodium salt. Supplied as lyophilized powder or pre-dissolved solution at user-specified concentration. |
| Storage Conditions | Lyophilized: store at -20 °C, desiccated, protected from light. Solution: store at -20 °C to -80 °C in single-use aliquots, protected from light. |
| Shelf Life | Lyophilized: 36 months at -20 °C. Reconstituted solution: 24 hours at 4 °C or 2 weeks at -20 °C (aliquoted). |
| Package Specifications | 100 mg, 500 mg, 1 g, 5 g, 25 g (lyophilized). Custom pre-weighed vials and bulk packaging available. |
| Product Form | White to pale yellow lyophilized powder. Hygroscopic. |
| Quality Control | HPLC purity, enzymatic activity with LDH standard, UV spectral analysis (A340/A260 ratio), moisture content, heavy metals analysis. |
| Key Features | Essential coenzyme for oxidoreductase assays; spectrophotometric detection at 340 nm for real-time kinetic monitoring; high purity suitable for sensitive clinical chemistry applications; cornerstone reagent for coupled enzyme assay systems. |
| Purity | >= 98% by HPLC at 260 nm. A340/A260 ratio >= 0.44. |
| Concentration | Lyophilized powder. Reconstitute at desired concentration. Typical stock: 10-100 mM. |
| Activity / Unit Definition | Enzymatically reducible by appropriate substrates with LDH (pyruvate to lactate), MDH (oxaloacetate to malate), ADH (acetaldehyde to ethanol). Rate proportional to enzyme concentration under saturating conditions. |
| Molecular Weight | 709.4 g/mol (disodium salt, beta-NADH). |
| Source / Origin | Produced via enzymatic reduction of NAD⁺ using formate dehydrogenase or alcohol dehydrogenase systems, or by fermentation using engineered microorganisms. Purified by ion-exchange chromatography. |
| pH Range / Optimal pH | Most stable at pH 7.0-9.0. Rapidly degrades in acidic conditions (pH <6.0). Working buffer pH typically 7.0-8.0 for optimal stability. |
| Shipping Conditions | Lyophilized: ambient temperature acceptable. Solution: ship on dry ice or with cold packs. |
| Expiration Date / Stability | 36 months (lyophilized, -20 °C). NADH in solution degrades via oxidation and hydrolysis; use freshly reconstituted for critical quantitative assays. |
| Regulatory / Compliance | ISO 9001 certified. Suitable for IVD clinical chemistry reagent formulation with appropriate quality grade selection. |
| Compatibility | Substrate for all NADH-dependent oxidoreductases. Compatible with Tris, phosphate, and HEPES buffers at pH 7.0-8.0. Not compatible with strong oxidizing agents. |
| Recommended Buffer System | Most stable in Tris or phosphate buffer, pH 7.5-8.5. Avoid carbonate buffers which promote NADH degradation. |
| Application Notes / Precautions | Protect from light and moisture. Reconstitute with deoxygenated buffer for maximum stability. Monitor A340 during storage to detect degradation. NADH solutions develop absorbance at 260 nm from decomposition products; the A340/A260 ratio is a quality indicator. |
| Batch-to-Batch Consistency | Lot-to-lot enzymatic activity within +/- 5% as measured by LDH kinetic assay. A340/A260 ratio >= 0.44 for all lots. |
For research use only, not for clinical use.
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