Recombinant Human FABP12 protein

Fatty Acid-Binding Protein 12 (FABP12) is a member of the fatty acid-binding protein family, a group of small intracellular lipid chaperones involved in the uptake, transport, and metabolism of hydrophobic ligands such as fatty acids, retinoids, and other lipid signaling molecules. While the biological functions of many FABP isoforms (e.g., FABP1 in the liver or FABP4 in adipocytes) are well characterized, FABP12 remains relatively understudied. It shares the conserved β-barrel structure typical of FABPs, with a molecular weight of approximately 15-16 kDa, and is thought to play roles in lipid homeostasis and cellular signaling pathways.

FABP12 was initially identified through genomic analyses, with its expression detected in specific tissues such as the testis and retina, suggesting potential tissue-specific functions. Recombinant FABP12 protein is engineered using heterologous expression systems (e.g., *E. coli* or mammalian cells) to enable functional and structural studies. This involves cloning the FABP12 gene into expression vectors, followed by protein purification using affinity chromatography (e.g., His-tag systems) and validation via SDS-PAGE or Western blot.

Current research focuses on elucidating FABP12’s ligand-binding specificity, interactions with cellular receptors, and its relevance to metabolic or degenerative diseases. For instance, its retinal expression hints at a possible role in visual metabolism, while testis-specific expression may link it to reproductive health. Recombinant FABP12 serves as a critical tool for *in vitro* assays, structural analysis (e.g., X-ray crystallography), and antibody production. However, challenges persist in fully mapping its physiological roles, signaling pathways, and therapeutic potential. Further studies are needed to clarify its contribution to lipid-related disorders or its utility as a biomarker or drug target.