Recombinant Human SLC16A3 protein

SLC16A3. also known as monocarboxylate transporter 4 (MCT4), is a member of the solute carrier family 16 (SLC16), which comprises proton-coupled transporters responsible for shuttling monocarboxylates such as lactate, pyruvate, and ketone bodies across cell membranes. This transmembrane protein plays a critical role in cellular metabolism by regulating the efflux of lactate, particularly in glycolytically active cells. Its expression is notably upregulated in hypoxic environments, such as tumor microenvironments, where cancer cells rely on aerobic glycolysis (the Warburg effect) to meet energy demands. SLC16A3-mediated lactate export helps maintain intracellular pH balance and supports metabolic symbiosis between tumor cells and adjacent stromal cells.

Recombinant SLC16A3 protein is engineered for research applications to study its structure, function, and interaction with potential inhibitors or therapeutic agents. Produced via heterologous expression systems (e.g., mammalian cells or bacteria), the recombinant protein retains key functional domains, including 12 predicted transmembrane helices and conserved substrate-binding sites. Its purification often involves affinity chromatography tags (e.g., His-tag) for ease of isolation. Studies using recombinant SLC16A3 have elucidated its kinetic properties, pH-dependent transport mechanisms, and role in diseases like cancer, diabetes, and inflammatory disorders. Additionally, it serves as a tool for drug screening, as targeting SLC16A3 may disrupt lactate-driven angiogenesis, immune evasion, or chemoresistance in tumors. Despite progress, challenges remain in achieving full-length, stable recombinant protein production due to its hydrophobic nature and complex membrane topology. Ongoing research aims to refine expression systems and crystallize the protein for advanced structural insights, which could accelerate the development of selective modulators for therapeutic interventions.