Lactoferrin (LTF) is an 80 kDa iron-binding glycoprotein belonging to the transferrin family, widely present in mammalian secretions such as milk, saliva, and tears, as well as in neutrophil granules. It plays a pivotal role in innate immunity, exhibiting antimicrobial, anti-inflammatory, and immunomodulatory properties by sequestering iron, disrupting microbial membranes, and interacting with host cell receptors. LTF antibodies, either polyclonal or monoclonal, are critical tools for detecting and quantifying lactoferrin in research and diagnostics. These antibodies enable techniques like ELISA, Western blotting, and immunohistochemistry to study LTF's expression, localization, and function in physiological and pathological contexts, including infections, inflammatory diseases, and cancer.
In clinical settings, LTF antibodies aid in diagnosing conditions marked by altered lactoferrin levels, such as dry eye syndrome, periodontitis, or inflammatory bowel disease. Additionally, they contribute to exploring LTF's dual role in cancer—either promoting or inhibiting tumor progression depending on the microenvironment. Recent studies also investigate lactoferrin's potential as a therapeutic agent or drug delivery vehicle, with antibodies serving to monitor its bioavailability and efficacy. Despite advancements, challenges remain in standardizing antibody specificity across species and applications, necessitating rigorous validation. Overall, LTF antibodies are indispensable for unraveling the protein's multifaceted roles and translational potential.