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 °C as supplied.
1 month, 2 to 8 °C under sterile conditions after reconstitution.
3 months, -20 to -70 °C under sterile conditions after reconstitution.
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.
Smathers, R & Petersen, D. (2011) Human Genomics 5:170.
Storch, J. & Thumser, AE. (2000) Biochim Biophys Acta. 1486:28.
Mihajlovic,M. & Lazaridis, T. (2007) Protein Sci. 9:2042.
Sweetser, D.A. et al. (1987) J. Biol. Chem. 262:16060.
Wang, G. et al. (2015) J Lipid Res. 56:2238.
Thompson, J. et al. (1997) J. Biol. Chem. 272:7140.
Bernlohr, DA. et al. (1997) Ann. Rev. of Nut. 17:277.
Huang, H. et al. (2015) Biochim Biophys Acta. 1851:946
Lowe J.B. et al. (1985) J. Biol. Chem. 260:3413.
Zimmerman, A.W. and J.H. Veerkamp (2002) Cell. Mol. Life Sci. 59:1096.
Haunerland, N.H. and F. Spener (2004) Prog. Lipid Res. 43:328.
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