FABP12 (fatty acid-binding protein 12) is an intracellular lipid chaperone that binds and transports fatty acids and lipid-related molecules throughout cellular compartments including the cytosol, mitochondria, and nucleus 1. As a member of the FABP family, FABP12 shares the characteristic structural features of FABPs: a water-filled interior-binding pocket surrounded by ten anti-parallel beta sheets forming a beta barrel, with regulatory alpha-helices at the superior surface 1. FABP12 is preferentially expressed in mammalian retina and testis 2, and is expressed in rat and mouse retinas with altered patterns in disease states 3. In prostate cancer, FABP12 drives metastatic transformation through the PPARγ signaling pathway, simultaneously inducing epithelial-to-mesenchymal transition (EMT) via Slug activation and enhancing lipid-derived energy production through increased fatty acid β-oxidation 4. FABP12 is preferentially amplified and overexpressed in metastatic compared to primary prostate tumors 4. The FABP12-Slug-Survivin axis mediates docetaxel chemoresistance by suppressing apoptosis and inhibiting programmed cell death, with high Survivin levels correlating to poor prognosis 5. Genomic analysis identified an FABP12 variant in familial trichoepithelioma patients, suggesting roles in hair follicle biology 6. A Mendelian randomization study revealed FABP12 has a protective causal relationship with anaphylactic shock from adverse drug reactions 7.