FABP1 Mouse

Fatty Acid Binding Protein-1 (FABP1), also known as liver-type fatty acid-binding protein (L-FABP), is a member of the fatty acid-binding protein family. These proteins are small, highly conserved cytoplasmic proteins that bind long-chain fatty acids and other hydrophobic ligands. FABP1 is primarily expressed in the liver but can also be found in the intestine, kidney, pancreas, stomach, and lung .

The fatty acid-binding proteins were initially discovered in 1972 through experiments using labeled oleate to identify a soluble fatty acid carrier in the enterocyte responsible for intestinal absorption of long-chain fatty acids . The human FABP1 gene is located on the short arm of chromosome 2, while the mouse FABP1 gene is located on chromosome 6 .

FABP1 has a unique structure compared to other members of the FABP family, allowing it to bind multiple ligands simultaneously. It has a larger solvent-accessible core, which enables more diverse substrate binding . The “portal hypothesis” suggests that fatty acids enter the solvent-accessible area of the protein through a dynamic region consisting of α-helix II and turns between the βC-βD and βE-βF loops. The fatty acid is then bound in the protein cavity for transport .

FABP1 plays a significant role in the binding, transport, and metabolism of long-chain fatty acids, endocannabinoids, phytocannabinoids, and other hydrophobic molecules . It is abundantly expressed in the liver, accounting for 7-11% of the total cytosolic protein . FABP1 is unique in its ability to bind a wide range of hydrophobic ligands, including bilirubin, monoglycerides, bile acids, and fatty acyl CoA .

Altered expression of FABP1 has been linked to various metabolic conditions, including obesity . The protein’s ability to bind and transport fatty acids and other hydrophobic molecules is crucial in preventing cytotoxicity by binding potentially toxic molecules when unbound .

Recombinant mouse FABP1 is used in research to study its structure, function, and role in various metabolic processes. The recombinant protein is produced using genetic engineering techniques, allowing researchers to investigate its interactions with different ligands and its impact on metabolic pathways.