Ferrochelatase (FECH) is a mitochondrial enzyme that catalyzes the final step in heme biosynthesis, inserting ferrous iron into protoporphyrin IX to form heme. It is encoded by the FECH gene and functions as a homodimer located in the mitochondrial matrix. Deficiencies or mutations in FECH are linked to erythropoietic protoporphyria (EPP), a rare genetic disorder characterized by photosensitivity and accumulation of protoporphyrin IX. FECH antibodies are essential tools for studying heme metabolism, mitochondrial disorders, and porphyria-related pathologies. These antibodies enable the detection and quantification of FECH protein levels in tissues or cells via techniques like Western blot, immunohistochemistry, and immunofluorescence. Research applications include investigating FECH's role in iron homeostasis, its interaction with mitochondrial transporters, and its potential involvement in diseases beyond EPP, such as certain anemias and cancers. Commercially available FECH antibodies are typically raised in rabbits or mice using recombinant protein fragments or synthetic peptides. Validation often involves knockout cell lines or tissue samples to confirm specificity. Recent studies also explore FECH's regulatory mechanisms under oxidative stress and its expression patterns in different cell types, emphasizing its broader impact on cellular health.