FABP4 is composed of a β-barrel structure that forms the lipid-binding site, and two α-helices that act as a lid on the β-barrel . This structure allows FABP4 to bind long-chain fatty acids and retinoic acid, facilitating their transport and metabolism within cells . The protein plays a crucial role in lipid transport, metabolism, insulin resistance, and angiogenesis .
The expression of FABP4 is induced by long-chain fatty acids and peroxisome proliferator-activated receptor γ (PPARγ) agonists . It is involved in various metabolic processes, and its dysregulation is associated with several metabolic disorders. For instance, knockout studies in mice have shown that the absence of FABP4 prevents the development of atherosclerosis and increases insulin sensitivity .
Elevated levels of FABP4 have been observed in patients with conditions such as colorectal cancer and rheumatoid arthritis . This makes FABP4 a potential biomarker for these diseases. Additionally, its role in metabolic processes makes it a target for therapeutic interventions aimed at treating metabolic disorders.
Recombinant human FABP4, tagged with a His tag, is produced in Escherichia coli (E. coli) and is typically used in research applications such as ELISA, Western blot (WB), and immunoprecipitation (IP) . The His tag facilitates the purification of the protein using standard chromatography techniques . This recombinant protein retains the functional properties of the native protein, making it a valuable tool for studying the biological functions and interactions of FABP4.