Recombinant Human CAT1 protein

CAT1 (Cationic Amino Acid Transporter 1), encoded by the *SLC7A1* gene in humans, is a critical membrane protein responsible for transporting cationic amino acids, such as arginine, lysine, and ornithine, across cell membranes. As a member of the solute carrier (SLC) family, CAT1 facilitates nutrient uptake and plays a vital role in cellular processes like nitric oxide synthesis, protein production, and cell proliferation. Its expression is particularly significant in endothelial cells, immune cells, and rapidly dividing tissues, linking it to vascular function, immune response, and cancer biology.

Recombinant CAT1 protein is produced using genetic engineering techniques to enable functional and structural studies. By expressing the *SLC7A1* gene in heterologous systems like mammalian cells (e.g., HEK293. CHO) or insect cells, researchers obtain purified CAT1 for investigating substrate specificity, transport mechanisms, and regulatory pathways. This recombinant approach also aids in developing assays to screen modulators targeting CAT1 activity, with potential therapeutic applications in diseases like hypertension (via nitric oxide regulation), cancer (by limiting arginine availability to tumor cells), and immune disorders.

Challenges in CAT1 recombinant production include maintaining proper membrane protein folding, post-translational modifications, and stability during purification. Advances in expression systems, detergent solubilization, and structural biology (e.g., cryo-EM) have improved yields and enabled detailed mechanistic insights. Current research focuses on CAT1’s role in metabolic reprogramming, drug resistance, and as a biomarker, highlighting its growing relevance in precision medicine and therapeutic development.