Recombinant Human H-FABP protein (His tag N-Terminus)

Supplementary information

This supplementary information is collated from multiple sources and compiled automatically.

H-FABP also known as heart-type fatty acid binding protein is a small protein with a molecular mass of approximately 14.5 kDa. This protein is primarily found in the cytoplasm of cardiac muscle cells but it also can be detected in skeletal muscles and other tissues at lower concentrations. H-FABP binds long-chain fatty acids and is important for the intracellular transport and metabolism of these molecules. The protein is often used as a biomarker for cardiac injury due to its rapid release into the bloodstream following muscle damage.

Biological function summary

Fatty acid binding largely defines H-FABP's role facilitating the transport of fatty acids within cells which is key for energy production. It is not part of a larger protein complex but plays into broader lipid metabolism processes. The efficiency of H-FABP in fatty acid binding and transport helps maintain cellular energy homeostasis especially in tissues with high fatty acid metabolism like the heart.

Pathways

H-FABP integrates into the fatty acid metabolic pathways and the beta-oxidation pathway. It is associated with the transport and utilization of fatty acids linking it to the peroxisome proliferator-activated receptor (PPAR) signaling pathway an important regulator of lipid metabolism. Proteins such as CD36 and PPARα interact with H-FABP within these pathways influencing lipid storage and energy balance.

Disruptions in H-FABP levels or function correlate with cardiovascular diseases including myocardial infarction. Elevated blood levels of H-FABP provide early markers of cardiac cell injury. Additionally alterations can also relate to metabolic disorders like obesity where lipid metabolism gets impaired. In these contexts proteins such as troponin and creatine kinase may also serve as biomarkers elucidating the relationship between H-FABP and myocardial stress or damage.