FABP3 Human, His

Fatty Acid Binding Protein 3 (FABP3), also known as Heart-type Fatty Acid Binding Protein (H-FABP), is a small cytoplasmic protein with a molecular weight of approximately 15 kDa . It is part of a larger family of fatty acid-binding proteins that play a crucial role in the intracellular transport and metabolism of long-chain fatty acids .

FABP3 is characterized by its ability to bind long-chain fatty acids and other hydrophobic ligands. The protein consists of a beta-barrel structure that forms a hydrophobic pocket, allowing it to sequester fatty acids within the cell . This binding capability is essential for the transport of fatty acids from the cell membrane to various intracellular organelles, including mitochondria, where they undergo beta-oxidation .

FABP3 is predominantly expressed in cardiac and skeletal muscle tissues, where it facilitates the efficient utilization of fatty acids as an energy source . Its expression is also noted in other tissues, albeit at lower levels. The high expression in cardiac tissue makes it a valuable biomarker for myocardial infarction, as it is rapidly released into the bloodstream following cardiac injury .

The recombinant form of FABP3, tagged with a hexahistidine (His) sequence, is produced using an expression system in Escherichia coli . The His tag facilitates the purification of the protein through affinity chromatography, ensuring a high degree of purity (>95%) . This recombinant protein is used extensively in research to study the binding properties and physiological roles of FABP3.

Recombinant FABP3 is utilized in various biochemical and immunological assays. Its ability to bind fatty acids makes it a useful tool for studying lipid metabolism and transport within cells . Additionally, its role as a biomarker for cardiac injury has led to its use in diagnostic assays for myocardial infarction .