Dihydrofolate reductase (DHFR) is a critical enzyme in cellular metabolism, catalyzing the reduction of dihydrofolate to tetrahydrofolate (THF), a vital cofactor in nucleotide synthesis and amino acid metabolism. DHFR plays a central role in DNA replication, cell proliferation, and one-carbon transfer reactions, making it a therapeutic target for cancer, autoimmune diseases, and infections. DHFR inhibitors, such as methotrexate and trimethoprim, are widely used as chemotherapeutic agents or antimicrobials.
DHFR antibodies are essential tools in biomedical research for detecting and quantifying DHFR expression. They are widely employed in techniques like Western blotting, immunohistochemistry (IHC), and immunofluorescence (IF) to study DHFR regulation in drug resistance, cancer progression, or folate metabolism disorders. For example, DHFR upregulation is associated with resistance to methotrexate in cancer cells, and antibodies help identify such mechanisms.
These antibodies are typically generated using recombinant DHFR proteins or peptide antigens, with monoclonal antibodies offering high specificity and polyclonal antibodies providing broader epitope recognition. Researchers also use DHFR antibodies to explore gene expression regulation, protein interactions, and subcellular localization. Commercial DHFR antibodies are often validated for cross-reactivity across species (human, mouse, rat) to support diverse experimental models. Their applications extend to drug development, biomarker discovery, and understanding folate-dependent pathways in diseases like neural tube defects or inflammatory conditions.