L-Malate Dehydrogenase (L-MDH)
ROCHE/LMDH-RO - from pig heart (mitochondrial)
Product Type: Chemical
| application(s) | life science and biopharma |
| biological source | Porcine heart (mitochondrial) |
| color | white |
| foreign activity | Fumarase <0.01% |
| GIDH 0.001% | |
| GOT 0.001% | |
| GPT 0.00185% | |
| LDH <0.01% | |
| NADH oxidase <0.001% | |
| form | solution |
| suspension | |
| manufacturer/tradename | Roche |
| NCBI accession no. | NM_001244153.1   |
| optimum pH | 7.4-7.5(reduction of oxaloacetate) |
| 9.2-9.5(oxidation of malate) | |
| packaging | pkg of 1 mL (10127248001 solution) |
| pkg of 1 mL (10127256001 suspension) | |
| pkg of 5 mL (10127914001suspension) | |
| Quality Level | 100 |
| shipped in | wet ice |
| solubility | water: miscible |
| specific activity | ~1200 units/mg protein (At 25 °C with oxaloacetate as the substrate.) |
| storage temp. | 2-8°C |
| suitability | suitable for Western blot |
| technique(s) | activity assay: suitable |
| UniProt accession no. | P00346 |
| Application: | The enzyme L-malate dehydrogenase from pig heart has been used to measure PEPCK (phosphoenolpyruvate carboxykinase) activity. The oxaloacetate, produced by PEPCK, is reduced to malate via the oxidation of NADH, which in turn is measured at 340 nm using a spectrophotometer. The enzyme has also been used to measure oxaloacetate by measuring the reduction in NADH spectroscopically at 340 nm. |
| Biochem/physiol Actions: | The enzyme L-malate dehydrogenase from pig heart catalyzes the oxidation of L-malate to oxaloacetate. The enzyme is an NAD-dependent mitochondrial dehydrogenase that functions in the tricarboxylic acid cycle. It is a component of the malate-aspartate shuttle that transports reducing equivalents across the inner mitochondrial membrane in the form of malate. |
| General description: | L-malate:NAD+ oxidoreductase The L-malate dehydrogenase enzyme is a nuclear gene product that is synthesized with a 24-residue amino-terminal signal peptide. This peptide is proteolytically cleaved during the translocation of the enzyme to the mitochondrial matrix. |
| Other Notes: | For life science research only. Not for use in diagnostic procedures. |
| Physical form: | Solution in 50% glycerol (v/v), pH approximately 7 |
| Physical form: | Suspension in 3.2 M ammonium sulfate solution, pH approximately 6 |
| Preparation Note: | Activator: – phosphate – arsenate – Mg2+ – Zn2+ |
| Quality: | Contaminants: <0.002% GOT, <0.01% fumarase and LDH, each luM each, <0.02% HK, <0.002% PGI |
| RIDADR | NONH for all modes of transport |
| WGK Germany | WGK 1 |
| Flash Point(F) | No data available |
| Flash Point(C) | No data available |
| activity | specific activity: ~1200 units/mg protein (At 25 °C with oxaloacetate as the substrate.) |
| Storage Temp. | 2-8°C; 2-8°C |
| Enzyme Commission (EC) Number | 1.1.1.37 ( BRENDA | IUBMB ) |
| UNSPSC | 12352200 |