This enzyme catalyzes the stereospecific interconversion of pyruvate and lactate, coupled with the simultaneous conversion of NADH to NAD+^+ or vice versa. It plays a crucial role in energy metabolism by maintaining the balance between glycolysis and fermentation. By regulating the levels of pyruvate, lactate, NADH, and NAD+^+, the enzyme ensures proper redox homeostasis and supports cellular energy requirements under varying metabolic conditions.
| Product Name | Recombinant Human L-Lactate Dehydrogenase A Chain (LDHA) |
| Accession | P00338 |
| Purity | Greater than 85% as determined by SDS-PAGE. |
| Host Species | Human |
| Gene | LDHA |
| Source | E.coli |
| Protein Expression Range | 5-323aa |
| Tag | Tag-Free |
| Molecular Mass | 35.1 kDa |
| Form | Liquid or Lyophilized powder |
| Buffer | Liquid form: default storage buffer is Tris/PBS-based buffer, 5%-50% glycerol. Lyophilized powder form: the buffer before lyophilization is Tris/PBS-based buffer, 6% Trehalose, pH 8.0. |
| Storage | 1. Store at -20¡«C/-80¡«C upon receipt, aliquoting is necessary for mutiple use. 2. Avoid repeated freeze-thaw cycles. 3. Store working aliquots at 4¡«C for up to one week. 4. In general, protein in liquid form is stable for up to 6 months at -20¡«C/-80¡«C. Protein in lyophilized powder form is stable for up to 12 months at -20¡«C/-80¡«C. |
