Mini Sample Human FABP2 (Intestinal Fatty Acid Binding Protein) ELISA Kit (E-MSEL-H0035)

This ELISA kit uses the Sandwich-ELISA principle. The micro ELISA plate provided in this kit has been pre-coated with an antibody specific to FABP2 . Standards or samples are added to the micro ELISA plate wells and combined with the specific antibody. Then a biotinylated detection antibody specific for FABP2 and Avidin-Horseradish Peroxidase (HRP) conjugate are added successively to each micro plate well and incubated. Free components are washed away. The substrate solution is added to each well. Only those wells that contain FABP2 , biotinylated detection antibody and Avidin-HRP conjugate will appear blue in color. The enzyme-substrate reaction is terminated by the addition of stop solution and the color turns yellow. The optical density (OD) is measured spectrophotometrically at a wavelength of 450 nm ± 35 nm. The OD value is proportional to the concentration of FABP2 . You can calculate the concentration of FABP2 in the samples by comparing the OD of the samples to the standard curve.

Fatty acid binding protein 2 (FABP2; I-FABP) is an intracellular protein composed of 127 amino acids, forming a small molecular structure. The tertiary structure of FABP is highly conserved, consisting mainly of 2 alpha helices and 10 antiparallel beta folded chains. This tertiary structure gives it specific binding affinity with fatty acids, facilitating their transport within cells. I-FABP is only expressed in intestinal cells and is a cytoplasmic protein expressed by mature intestinal cells at the tips of small intestinal villi, accounting for approximately 2% of the intracellular protein in mature intestinal cells. Its gene contains three introns and four exons, located on chromosome 4 g28-q31. The exons are relatively short, with the shortest exon 4 encoding about 16-17 amino acids and the longest exon 2 encoding about 60 amino acids. The tertiary structure of I-FABP is similar to that of other subtypes of fatty acid binding proteins. Its semi flattened cylindrical outer cavity is composed of 10 anti parallel β - folded chains, and the inner cavity is filled with two short α - helix structures. However, unlike other families of fatty acid binding proteins, this core filling structure is the site where I-FABP binds to long-chain fatty acids. The structure of I-FABP contains a fatty acid binding pocket that can bind to fatty acids and promote their transport into intestinal mucosal cells; Its expression level in the intestine is related to the absorption and metabolism of fatty acids.The function of I-FABP is not limited to fatty acid transport, but also participates in other biological processes such as intestinal diseases, inflammatory responses, cell apoptosis, and tumorigenesis. In addition, the expression level of I-FABP is also closely related to the occurrence and development of many metabolic diseases, such as obesity, diabetes and cardiovascular diseases.