Recombinant Human FABP1/L-FABP Protein, CF

Recombinant Human FABP1/L-FABP Protein, CF Summary

Product Specifications

Product Datasheets

Carrier Free

CF stands for Carrier Free (CF). We typically add Bovine Serum Albumin (BSA) as a carrier protein to our recombinant proteins. Adding a carrier protein enhances protein stability, increases shelf-life, and allows the recombinant protein to be stored at a more dilute concentration. The carrier free version does not contain BSA.

In general, we advise purchasing the recombinant protein with BSA for use in cell or tissue culture, or as an ELISA standard. In contrast, the carrier free protein is recommended for applications, in which the presence of BSA could interfere.

Background: FABP1/L-FABP

Fatty acid binding protein-1 (FABP1; also named L- or liver FABP, hepatic FABP, Z protein, and heme-binding protein) is a member of a large superfamily of lipid binding proteins that are expressed in a tissue specific manner (1, 10, 11). FABP1 is one of ten cytoplasmic FABPs that are 14-15 kDa in size and range from 126‑140 amino acids (aa) in length (1, 2, 3). Although all are highly conserved in their tertiary structure, there is only modest aa identity between any two members. The FABP family members are subdivided based on organ or tissue type it was originally expressed or identified; 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-FABP (T-FABP) (1). Human L-FABP, the product of the FABP1 gene, is a 127 aa cytosolic protein that shows a flattened beta -barrel structure generated by a series of antiparallel beta -strands and two alpha ‑helices (4, 7). Unlike other members in the FABP family, each molecule of FABP1 is capable of binding two molecules of long-chain fatty acids. Other ligands may include heme, steroids, acyl CoAs, oxidized/peroxidized fatty acids, leukotrienes, prostaglandins and peroxisome proliferators (5, 6, 7, 13). It is suggested that ligands first bind to the outside of the molecule, and this binding subsequently induces a conformational change in the binding protein, resulting in "internalization" of the ligand (7, 12). An Ala-to-Thr polymorphism at position # 54 has been associated with an increased risk of type II diabetes (7, 10) and a Thr-to-Ala polymorphism at position # 94 has been reported to increase cholesterol binding affinity (8). Human FABP1 is 84%, 82% and 90% aa identical to mouse, rat and canine FABP1, respectively (9). It also shows 29% and 24% aa identity to human H-FABP and I‑FABP, respectively.

Related Research Areas

• Definitive Endoderm Markers
• Early Endodermal Lineage Markers
• Hepatic Endoderm
• Hepatic Endoderm Cell Markers
• Lipid and Fatty Acid Transport
• Lipid/Cholesterol Metabolism
• Obesity
• Renal Markers