L-Lactate Dehydrogenase (LDHA)

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.

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 (L-lactate dehydrogenase A chain) is responsible for the conversion of pyruvate to lactate, the final step of glycolysis. It is overexpressed in various cancers. In cancer cells, HIF-1a (hypoxia-inducible factor) induces the expression of LDHA, which helps in maintaining glycolysis in cells.

L-lactic dehydrogenase catalyzes the conversion of L-lactate into L-pyruvate while reducing NAD⁺ to NADH and H⁺.

Research area: Cell Signaling
The gene LDHA (L-lactate dehydrogenase A chain) is mapped to human chromosome 11p15. It is a subunit of lactate dehydrogenase.In particular, lactic dehydrogenase A (LDHA) is mainly found in skeletal muscle, and for that reason is known as the M subunit. This recombinant form of LDHA has a C-terminal histidine-tag.

One unit will reduce 1.0 μmole of pyruvate to L-lactate per min at pH 7.5 at 37 °C.

Buffered aqueous solution with Hepes (pH 7.5), NaCl and glycerol.