FABP1 Rat

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 involved in the binding, transport, and metabolism of long-chain fatty acids (LCFAs) and other hydrophobic molecules .

The fatty acid-binding proteins (FABPs) 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 LCFAs . 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 allows for more diverse substrate binding .

FABP1 is primarily expressed in the liver, where it accounts for 7-11% of the total cytosolic protein . It is also found in the intestine, kidney, pancreas, stomach, and lung . FABP1 binds and transports LCFAs, endocannabinoids, phytocannabinoids, and other hydrophobic molecules . It plays a significant role in preventing cytotoxicity by binding potentially toxic molecules such as heme and fatty acids .

Recombinant rat FABP1 is a form of the protein that has been produced through recombinant DNA technology. This allows for the study of the protein’s function and structure in a controlled environment. Rat FABP1 is well-studied and has been shown to have significant roles in lipid metabolism and the endocannabinoid system .

Altered expression of FABP1 has been linked to various metabolic conditions, including obesity and non-alcoholic fatty liver disease (NAFLD) . In humans, a single nucleotide polymorphism (SNP) resulting in a T94A substitution in FABP1 is associated with altered body mass index (BMI), elevated plasma triglycerides, LDL cholesterol, and atherothrombotic cerebral infarction .