Rat intestinal fatty acid binding protein,iFABP ELISA Kit

FABP are thought to play a role in the intracellular transport of long-chain fatty acids and their acyl-CoA esters. FABP2 is probably involved in triglyceride-rich lipoprotein synthesis. Binds saturated long-chain fatty acids with a high affinity, but binds with a lower affinity to unsaturated long-chain fatty acids. FABP2 may also help maintain energy homeostasis by functioning as a lipid sensor.

1. Study characterized internal-water exchange and associated conformational dynamics in rIFABP by recording the water 2H and 17O MRD profiles for the apo and palmitate-bound forms PMID: 26012957
2. This work highlights the importance of the beta-barrel of IFABP for its specific functions. PMID: 25311169
3. the portal region of IFABP penetrates deeply into the phospholipid bilayer, especially when CL-containing vesicles are employed. The orientation of the protein and the degree of penetration were highly dependent on the lipid composition PMID: 24148314
4. n-3 PUFAs protect the intestinal barrier by modifying intracellular I-FABP, activating the PPARgamma pathway, and then upregulating tight junction protein expression. PMID: 22554584
5. Conjugated linoleic acid can improve insulin resistance of obese rat and increase the expression of fatty acid binding protein 2 mRNA. PMID: 16921753
6. Delta 78 Delta beta-barrel motif retains substantial beta-sheet content and preserves tertiary interactions, displaying cooperative unfolding and binding activity. Most strikingly, this construct adopts a remarkably stable dimeric structure in solution. PMID: 19844951
7. simulations of apo and holo-fatty acid binding protein: structure and dynamics of protein, ligand and internal water PMID: 11812142
8. Exchanging the alpha-helical domain of intestinal FABP (IFABP) for that of liver FABP drastically modifies the collisional mechanism characteristic of IFABP. PMID: 15035630
9. Increased concentrations of H-FABP significantly correlated with the concentrations of TNF- alpha in chronic heart failuare. PMID: 15277733
10. An examination of types of intermediates that are observed during the folding of this protein. PMID: 15723553
11. ionic interactions between IFABP and membranes appear to play a primary role in the process of fatty acid transfer to membranes, and hydrophobic interactions can also modulate the rates of ligand transfer PMID: 15863832
12. FABP2 gene polymorphism is associated in patients diagnosed with carotid artery atheroscelrosis. PMID: 16013194
13. analysis of intestinal fatty acid-binding protein stability and unfolding PMID: 16162507
14. there may be different collisional complex structures for holo- and apo-IFABP PMID: 16551626
15. The Gly121Val mutation of IFABP slows the formation of a normal nucleating site, not only slowing overall folding, but also allowing intermediates in regions distant from the mutation to be experimentally observed. PMID: 17615232
16. alphaI-helix is crucial for IFABP collisional FA transfer, and further indicate the participation of the alphaII-helix in the formation of a protein-membrane "collisional complex". PMID: 18284926
17. A structural explanation of the observed affinity of rat I-FABP for different drugs based on spectroscopic data and modeling experiments is presented.immunocytochemistry has been used to probe the expression of I-FABP in a cell culture model. PMID: 19160019
18. Delta98Delta (encompassing residues 29-126) emerges as a monomeric variant of intestinal fatty acid binding protein that folds properly, retaining functional activity, despite lacking extensive stretches involved in the closure of the beta-barrel. PMID: 19309727

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Cytoplasm.

Calycin superfamily, Fatty-acid binding protein (FABP) family

Expressed in the small intestine. Expression in the mucosal cells of the ileum extends from the midvillar region to the villus tips.

KEGG: rno:25598

UniGene: Rn.91358