Fatty acid-binding protein 12 (FABP12) is a member of the FABP family, which comprises intracellular lipid chaperones involved in fatty acid uptake, transport, and metabolic regulation. While extensively studied members like FABP4 (adipocyte) or FABP1 (liver) are well-characterized, FABP12 remains less understood. It shares the conserved β-barrel structure typical of FABPs, enabling hydrophobic ligand binding, but exhibits distinct tissue expression patterns. Emerging evidence suggests FABP12 may localize to tissues such as testis, adipose, or intestinal regions, though its precise distribution and physiological roles require further validation.
FABP12 antibodies are critical tools for investigating its expression, subcellular localization, and interaction networks. Polyclonal antibodies often target unique peptide sequences within its variable regions to ensure specificity, while monoclonal antibodies enable reproducible detection in assays like Western blot, immunohistochemistry, or immunofluorescence. These reagents help elucidate FABP12's potential roles in lipid metabolism, cellular signaling, or disease contexts. For instance, dysregulation of FABPs is linked to metabolic disorders, inflammation, and cancer, making FABP12 a candidate biomarker or therapeutic target.
However, challenges persist due to FABP12's structural homology with other family members, necessitating rigorous antibody validation via knockout controls or epitope mapping. Current research focuses on clarifying its ligand preferences, tissue-specific functions, and relevance in pathologies. Reliable FABP12 antibodies thus remain pivotal for advancing its biological and clinical characterization.