BACKGROUND Fatty acid-binding proteins (FABPs) are members of the superfamily of lipid-binding proteins (LBP). So far 9 different FABPs, with tissue-specific distribution, have been identified: L (liver), I (intestinal), H (muscle and heart), A (adipocyte), E (epidermal), Il (ileal), B (brain),M(myelin) and T (testis). The primary role of all the FABP family members is regulation of fatty acid uptake and intracellular transport. The structure of all FABPs is similar – the basic motif characterizing these proteins is beta-barrel, and a single ligand (e.g. a fatty acid, cholesterol, or retinoid) is bound in its internal water-filled cavity. Despite the wide variance in the protein sequence, the gene structure is identical. The FABP genes consist of 4 exons and 3 introns and a few of them are located in the same chromosomal region. For example, A-FABP, E-FABP and M-FABP create a gene cluster.1 Physiological roles of these proteins are not only involved in FA transport, but also in regulation of cell growth and differentiation, cellular signalling, gene transcription and cytoprotection.2 Because of their physiological properties some FABP genes were tested in order to identify mutations altering lipid metabolism and relating with other diseases.
Long-chain free fatty acids, a major hydrolysis product of dietary triglycerides, are absorbed from the lumen into polarized enterocytes that line the small intestine. Following apical absorption into the enterocytes, free fatty acids are reincorporated into triglycerides, which are secreted basolaterally as chylomicrons. The intestinal fatty acid binding protein (IFABP, or FABP-2) is a small (15 kDa), highly abundant protein expressed solely in enterocytes of the proximal small intestine. IFABP has been shown to bind both saturated and unsaturated long-chain fatty acids in vitro. Several functions for IFABP have been proposed, which have included the facilitation of cellular uptake and/or transport of long-chain fatty acids within enterocytes. It was shown that the IFABP/FABP2 A54T missense mutation may contribute to the triglyceride enrichment of HDL in the postprandial state that, in turn, may alter the risk of atherosclerotic vascular disease.3
1. Merkel, M. Et al: J. Biol. Chem. 277:7405-11, 2001 2. Hamilton, M.T. et al: Am J Physiol Endocrinol Metab 275: E1016-E1022, 1998 3. Kamei, Y. et al: Biochem. Int. 26:923-34, 1992
Products are for research use only. They are not intended for human, animal, or diagnostic applications.
Purified recombinant human FABP-2 fragments expressed in E. coli.
Species & predicted
reactivity ( ):
Human, Mouse, Rat
Weight of protein:
Detects endogenous FABP-2 proteins without cross-reactivity with other family members.
Store at -20°C, 4°C for frequent use. Avoid repeated freeze-thaw cycles.
*Optimal working dilutions must be determined by end user.