D-Lactic Dehydrogenase from Lactobacillus leichmannii
SIGMA/L2011 - ammonium sulfate suspension, ≥250 units/mg protein (biuret)
Synonym: Lactate; (R)-Lactate:NAD+ oxidoreductase; D−LDH
CAS Number: 9028-36-8
MDL Number: MFCD00130907
Product Type: Chemical
Unit Definition One unit will reduce 1.0 μmole of pyruvate to D-lactate per min at pH 7.0 at 25 °C.
| foreign activity | Malic dehydrogenase <0.5% of base activity |
| form | ammonium sulfate suspension |
| Quality Level | 200  |
| specific activity | ≥250 units/mg protein (biuret) |
| storage temp. | 2-8°C |
| Biochem/physiol Actions: | Lactic dehydrogenase (LDH)plays an important role in the glycolytic pathway where it converts pyruvate tolactate by using NAD+ as a co-factor. It is considered animportant molecule that can be used in cancer therapy as it acts as aglycolytic inhibitor. Inhibition of LDH is associated with blocking of aerobicglycolysis in tumour cells. |
| General description: | Research area: Cell Signalling D-lactate dehydrogenase belongs to the D-isomer-specific 2-hydroxyacid dehydrogenase family. Lactate dehydrogenase (LD) is a tetramer consisting of two (H and M) subunits. It has five isozymes (LD1 to LD5) and this composition varies in different tissues. LD1 is abundant in the kidney, heart, and erythrocytes. LD5 is found in the liver and skeletal muscles. LD is a ubiquitous molecule found in plants, yeast, mammals, and microorganisms and is a member of the oxidoreductase family. |
| Other Notes: | One unit will reduce 1.0 μmole of pyruvate to |
| Packaging: | 2500, 5000 units in glass bottle |
| Physical form: | Suspension in 3.2 M (NH4)2SO4, pH 6.0 |
| RIDADR | NONH for all modes of transport |
| WGK Germany | WGK 1 |
| Flash Point(F) | Not applicable |
| Flash Point(C) | Not applicable |
| activity | specific activity: ≥250 units/mg protein (biuret) |
| Storage Temp. | 2-8°C |
| Enzyme Commission (EC) Number | 1.1.1.28 ( BRENDA  | IUBMB ) |
| UNSPSC | 12352204 |