Formulation Lyophilized from a 0.2 μm filtered solution in PBS, EDTA and DTT.
Reconstitution Reconstitute at 1 mg/mL in PBS.
Shipping The product is shipped at ambient temperature. Upon receipt, store it immediately at the temperature recommended below.
Stability & Storage:Use a manual defrost freezer and avoid repeated freeze-thaw cycles.
12 months from date of receipt, -20 to -70 degreesC as supplied. 1 month, 2 to 8 degreesC under sterile conditions after reconstitution. 3 months, -20 to -70 degreesC under sterile conditions after reconstitution.
R&D Systems proteins are almost always sold with a bioassay to indicate activity. However, we recognize that sometimes proteins might be novel, and their bioactivity may not be well understood. In addition, some researchers may wish to use polypeptides to make antibodies. To facilitate the advancement of new science, we now offer our Innovator Series of proteins.
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.
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