L-Lactate Dehydrogenase (LDHA)
SIGMA/SAE0049 - from human, recombinant, expressed in E. coli, aqueous solution
Synonym: Lactic Dehydrogenase, recombinant from E. coli; α-HBDH; α-hydroxy butyratede hydrogenase; anaerobic lactate dehydrogenase; (S)-Lactate: NAD+ oxidoreductase; L-Lactate Dehydrogenase; Lactate
CAS Number: 9001-60-9
MDL Number: MFCD00131466
Product Type: Chemical
| biological source | human |
| color | colorless |
| form | aqueous solution |
| Quality Level | 200 ![]() |
| recombinant | expressed in E. coli |
| shipped in | dry ice |
| storage condition | (Keep container tightly closed in a dry and well-ventilated place) |
| storage temp. | −20°C |
| UniProt accession no. | K1T0A2 ![]() |
| Application: | L-Lactate Dehydrogenase (LDHA) has been used in in vitro phosphoglycerate mutase 1 (PGAM1) inhibitors screening assay. It has also been used in a colorimetric assay for determining lactate concentration in conditioned media. |
| Biochem/physiol Actions: | L-lactic dehydrogenase catalyzes the conversion of L-lactate into L-pyruvate while reducing NAD+ to NADH and H+. L-lactate dehydrogenase A chain (LDHA), an enzyme involved in pyruvate metabolism, LDH is responsible for the conversion of pyruvate to lactate, the final step of glycolysis. It is overexpressed in various cancers. LDHA regulates the microenvironment of developing tumors by the hypoxia-inducible factor (HIF)-signaling pathway. LDHA aids in the NAD+ regeneration during the β-oxidation of fatty acid. LDHA ( |
| Biochem/physiol Actions: | |
| General description: | |
| Other Notes: | One unit will reduce 1.0 μmole of pyruvate to L-lactate per min at pH 7.5 at 37 °C. |
| Physical form: | Buffered aqueous solution with Hepes (pH 7.5), NaCl and glycerol. |
| RIDADR | NONH for all modes of transport |
| WGK Germany | WGK 1 |
| Flash Point(F) | Not applicable |
| Flash Point(C) | Not applicable |
| Storage Temp. | −20°C |
| Enzyme Commission (EC) Number | 1.1.1.27 ( BRENDA ![]() ![]() |
| UNSPSC | 12352200 |

