FABP1 Human, His

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 .

FABP1 is composed of ten antiparallel beta strands that form a barrel structure with a larger binding pocket compared to other FABPs. This unique structure allows FABP1 to accommodate multiple ligands simultaneously . The protein has a molecular weight of approximately 18.71 kDa and contains an N-terminal hexahistidine (His) tag, which facilitates its purification and detection in research applications .

The primary role of FABP1 is to facilitate the uptake, transport, and metabolism of long-chain fatty acids (LCFAs) and other hydrophobic molecules . It is also capable of binding bile acids, bilirubin, monoglycerides, and fatty acyl CoA . FABP1 plays a significant role in preventing cytotoxicity by binding potentially toxic molecules when they are unbound .

Recombinant FABP1 is produced using an expression system, typically in E. coli, and is purified to a high degree of purity (>95%) using SDS-PAGE under reducing conditions . The recombinant protein is often used as a positive control in various immunological assays, including Western Blot .

Recombinant FABP1 is widely used in research to study fatty acid metabolism, transport, and related metabolic conditions such as obesity and hepatocellular adenoma . Its ability to bind a wide range of hydrophobic ligands makes it a valuable tool for investigating the mechanisms of fatty acid transport and metabolism in different tissues .