LDHA Rat

LDHA is a homotetrameric enzyme, meaning it consists of four identical subunits. Each subunit has an active site where the conversion of pyruvate to lactate occurs. The enzyme is highly conserved across species, including rats, humans, and other mammals . In rats, recombinant LDHA is often produced using bacterial expression systems like E. coli, which allows for the efficient production and purification of the enzyme .

LDHA plays a pivotal role in maintaining the balance between glycolysis and oxidative phosphorylation. During intense exercise or in hypoxic conditions, cells rely on anaerobic glycolysis to meet their energy demands. LDHA facilitates this process by regenerating NAD+, which is necessary for the continuation of glycolysis .

LDHA is not only important for normal cellular metabolism but also has significant implications in various diseases. Elevated levels of LDHA are often observed in cancer cells, where it supports the Warburg effect—a phenomenon where cancer cells preferentially utilize glycolysis over oxidative phosphorylation, even in the presence of oxygen . This makes LDHA a potential target for cancer therapy, as inhibiting its activity could disrupt the metabolic flexibility of cancer cells.

Recombinant rat LDHA is typically produced using automated protocols that involve bacterial expression systems. One such method uses the ÄKTAxpress™ chromatography system, which allows for the efficient purification of milligram quantities of untagged recombinant LDHA. This process involves cation exchange followed by size exclusion chromatography, resulting in high-purity enzyme suitable for structural and ligand-binding studies .

Recombinant LDHA is widely used in biochemical research to study enzyme kinetics, metabolic pathways, and drug interactions. Its role in cancer metabolism makes it a valuable tool for screening potential inhibitors that could serve as therapeutic agents .