Recombinant Proteins
Product List
FABP12 Human
Fatty Acid Binding Protein-12 Human Recombinant
FABP2 Human
Fatty Acid Binding Protein-2 Human Recombinant
FABP2 Human, His
Fatty Acid Binding Protein 2 Human Recombinant, His Tag
PMP2 Human, His
Peripheral Myelin Protein-2 Human Recombinant, His Tag
FABP4 Human
Fatty Acid Binding Protein 4 Human
FABP4 Human, His
Fatty Acid Binding Protein 4 Human Recombinant, His Tag
FABP1 Mouse, His
Fatty Acid Binding Protein-1, His Tag Mouse Recombinant
FABP1 Rat
Fatty Acid Binding Protein-1 Rat Recombinant
FABP7 Human
Fatty Acid Binding Protein-7 Human Recombinant
FABP7 Human, His
Fatty Acid Binding Protein-7 Human Recombinant, His Tag
Introduction
Fatty acid-binding proteins (FABPs) are a family of low-molecular-weight intracellular proteins that bind to hydrophobic ligands, primarily fatty acids. These proteins play a crucial role in the transport and metabolism of fatty acids within cells . FABPs are classified into several types based on their tissue-specific expression, including liver (L-FABP), intestine (I-FABP), heart (H-FABP), adipocyte (A-FABP), epidermal (E-FABP), ileal (Il-FABP), brain (B-FABP), myelin (M-FABP), and testis (T-FABP) .
FABPs are small, structurally conserved cytosolic proteins with a water-filled interior-binding pocket surrounded by ten anti-parallel beta sheets, forming a beta barrel . They are ubiquitously expressed in tissues that are highly active in fatty acid metabolism, such as the liver, intestine, heart, adipose tissue, and brain . The expression patterns of FABPs are tissue-specific, with each type predominantly expressed in certain tissues but not exclusively limited to them .
The primary function of FABPs is to bind fatty acids and facilitate their transport within cells . They enhance the solubility of hydrophobic fatty acids, allowing their efficient transport within the aqueous cytoplasm . FABPs also play a role in immune responses and pathogen recognition by modulating lipid-mediated signaling pathways . They are involved in various cellular processes, including signal transduction, lipid droplet storage, trafficking, membrane synthesis, and lipid-mediated transcriptional regulation .
FABPs function as cytoplasmic lipid chaperones, facilitating fatty acid solubilization, trafficking, and metabolism . They interact with various membrane and intracellular proteins, such as peroxisome proliferator-activated receptors (PPARs) and hormone-sensitive lipase (HSL), to regulate tissue and cellular-specific lipid responses . By transporting fatty acids to the nucleus, FABPs can modulate the activity of nuclear receptors involved in transcriptional regulation .
The expression and activity of FABPs are regulated by various mechanisms, including transcriptional regulation and post-translational modifications . For example, the expression of FABP1 is regulated by PPAR isoforms, with PPARα and PPARβ agonists inhibiting its expression, while PPARγ agonists increase its expression . Post-translational modifications, such as phosphorylation, can also influence the activity and function of FABPs .
FABPs have several applications in biomedical research, diagnostic tools, and therapeutic strategies . They serve as biomarkers for disease diagnosis and prognosis, particularly in cardiovascular diseases where elevated levels of heart-type FABP (H-FABP) in blood plasma are associated with acute myocardial infarction . FABPs are also being explored as potential therapeutic targets for metabolic disorders, cancer, and neurological diseases .
Throughout the life cycle, FABPs play a critical role in development, aging, and disease . They are involved in the regulation of lipid metabolism and energy homeostasis, which are essential for growth and development . During aging, the levels of FABPs decline, which may contribute to age-associated decline in synaptic activity and other metabolic processes . In disease states, such as metabolic syndrome and cancer, FABPs are often dysregulated, highlighting their importance in maintaining cellular homeostasis .
