Recombinant Human SLC19A2 protein

SLC19A2 recombinant protein is derived from the SLC19A2 gene, which encodes a high-affinity thiamine (vitamin B1) transporter critical for cellular uptake of this essential micronutrient. As a member of the solute carrier family 19. SLC19A2 is primarily expressed in metabolically active tissues, including the intestine, liver, pancreas, and placenta. It localizes to both the plasma membrane and mitochondrial membrane, facilitating thiamine transport to support energy metabolism and biosynthesis pathways. Mutations in SLC19A2 are linked to thiamine-responsive megaloblastic anemia (TRMA), a rare autosomal recessive disorder characterized by anemia, diabetes mellitus, and sensorineural deafness.

Recombinant SLC19A2 protein is produced using heterologous expression systems (e.g., mammalian cells, bacteria, or yeast) to study its structure-function relationships, substrate specificity, and interaction with therapeutic agents. Researchers employ this engineered protein to investigate molecular mechanisms underlying TRMA pathogenesis, including impaired thiamine absorption and mitochondrial dysfunction. It also serves as a tool for drug screening to identify compounds that modulate transporter activity or stabilize mutant variants. Additionally, recombinant SLC19A2 aids in elucidating tissue-specific regulatory mechanisms of thiamine homeostasis and its broader role in neurological and metabolic health. Recent studies have explored its potential as a biomarker or therapeutic target for conditions associated with thiamine deficiency, such as diabetes complications and neurodegenerative diseases. The protein’s recombinant form enables standardized in vitro assays, overcoming challenges posed by low native expression levels in biological samples. Ongoing research focuses on optimizing its stability and functional reconstitution in membrane models to advance translational applications.