FABP, HUMAN

Fatty acid binding protein 1 (FABP1) is one of nine known cytosolic fatty acid binding proteins ranging in size from 14-15 kDa containing 127-132 amino acids. Members of this protein family exhibit high affinity for small lipophilic ligands and were named according to the tissue from which they were initially isolated. Studies suggest that FABPs are involved in the uptake and metabolism of fatty acids, in the maintenance of cellular membrane fatty acid levels, in intracellular trafficking of these substrates, in the modulation of specific enzymes of lipid metabolic pathways, and in the modulation of cell growth and differentiation. FABP family members have highly conserved three dimensional structures and 22-73% amino acid sequence similarity. FABP1 is composed of ten antiparallel β strands that form a barrel and have a bigger binding pocket than the other FABPs allowing it to accommodate two fatty acids into its binding pocket. Expression of FABP1 is decreased in hepatoblastoma and hepatocellular carcinoma making the protein a potential tumor marker. Moreover, studies have suggested FABP1 as a potential biomarker for both liver and kidney injury.

The Human FABP4 produced from Human Adipose Tissue has a molecular mass of 14.587kDa (calculated without glycosylation) containing 131 amino acid residues.

Escherichia Coli

The amino acid sequence of the recombinant human FABP5 is 100% homologous to the amino acid sequence of the human FABP-5.

Human Fatty Epidermal Acid Binding Protein FABP also called FABP-5 is a 15 kD member of the intracellular fatty acid binding protein (FABP) family, which is known for the ability to bind fatty acids and related compounds ( bile acids or retinoids). In an internal cavity. The fatty acid binding proteins aP2 (fatty acid binding protein [FABP]-4) and mal1 (EFABP) are closely related and both are expressed in adipocytes. 

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