SLC1A5. also known as ASCT2 (alanine-serine-cysteine transporter 2), is a sodium-dependent neutral amino acid transporter primarily responsible for the uptake of glutamine, alanine, serine, and other small neutral amino acids. It belongs to the solute carrier family 1 (SLC1) and plays a critical role in cellular metabolism, particularly in cancer cells that rely on glutamine for energy production and biosynthesis (a phenomenon termed "glutamine addiction"). SLC1A5 is overexpressed in various malignancies, including breast, lung, and colorectal cancers, making it a potential biomarker and therapeutic target.
Antibodies targeting SLC1A5 are widely used in research to study its expression, localization, and function in normal and pathological conditions. These antibodies enable detection via techniques like Western blotting, immunohistochemistry (IHC), and immunofluorescence (IF), helping to correlate SLC1A5 levels with tumor progression, metabolic reprogramming, and patient prognosis. Additionally, SLC1A5-blocking antibodies are being explored in preclinical studies to inhibit glutamine uptake, thereby starving cancer cells of nutrients and suppressing tumor growth. Challenges in antibody development include ensuring specificity due to structural similarities among SLC transporters. Recent studies also investigate its role in viral entry (e.g., as a receptor for some retroviruses), broadening its biomedical relevance.